CN115651071A

CN115651071A - Antigen fragment and truncation of recombinant protein of feline herpesvirus type I HR-1 strain and application of antigen fragment and truncation in vaccine

Info

Publication number: CN115651071A
Application number: CN202211011293.4A
Authority: CN
Inventors: 查丽莎; 郑琪
Original assignee: Shenzhen Hertz Life Science Technology Co ltd
Current assignee: Shenzhen Hertz Life Science Technology Co ltd
Priority date: 2022-08-23
Filing date: 2022-08-23
Publication date: 2023-01-31
Also published as: CN117843733A

Abstract

The invention provides an antigen fragment and a truncation of a recombinant protein of a feline herpesvirus type I HR-1 strain and application thereof in vaccines, belonging to the technical field of vaccines. In the traditional vaccine, gB and gD proteins are adopted to prepare the vaccine, the gC, gD and gE composition is selected and truncated to obtain the recombinant protein, and the prepared vaccine has the advantages of excellent quality, high immune efficacy, stable immune effect, low cost, immune protection in a shorter time and the like, and is obviously superior to the traditional vaccine.

Description

Antigen fragment and truncation of recombinant protein of feline herpesvirus type I HR-1 strain and application of antigen fragment and truncation in vaccine

Technical Field

The invention relates to the technical field of vaccines, in particular to an antigen fragment and a truncation of a recombinant protein of a feline herpesvirus type I HR-1 strain and application thereof in vaccines.

Background

Feline herpes virus I type (Felinehersvirus-1, FHV-1) is a linear double-stranded DNA enveloped virus, belongs to the family of herpesviridae, and belongs to the subfamily of alpha-herpesviridae. FHV-1, one of the major pathogens responsible for the development of respiratory and ocular diseases in felines, poses a serious health hazard to felines, especially susceptible kittens, with mortality rates as high as 50%.

FHV-1 is replicated at the nasal, tracheal and conjunctiva parts of kittens after infecting kittens, expels toxin to the outside through secretion of eyes and noses, can cause acute or chronic infection of kittens, causes inflammation of upper respiratory tract and eyes, causes hair loss around eyes and noses under the stimulation of purulent secretion to cause scabbing, and even leads cats with serious illness to have symptoms such as atrophy and deformation of turbinates, blindness and the like. The infected cat can establish a latent period, FHV-1 is latent in the trigeminal ganglion and the visual ganglion of the recovered cat, and is easy to cause repeated infection under the influence of external environmental factors of the cat house, such as large population density, high turnover rate and different sources, so that the disease is not favorably prevented and controlled.

Currently, FHV-1 is prevalent worldwide, and China has isolated the virus in many areas and made significant progress in pathogenic mechanisms, epidemiology, diagnosis and detection, etc. Vaccines are important means for controlling infectious diseases. However, FHV-1 vaccines have been reported so far, and no specific drug for treating FHV-1 disease has been found.

Vaccination is the primary means of preventing FHV-1 infection. Existing studies support the use of inactivated vaccines or FVRCP vaccine products in acute FHV-1 infected cats. Modified live (mLV) and inactivated vaccines are now commercially available, however the vaccines only reduce clinical symptoms and do not prevent viral shedding or establish field viral latency.

The gB glycoprotein, gp143/108 in virus-infected cells, was 108, 70, 64 and 58kDa under denaturing conditions. Among these proteins, the 108kDa glycoprotein FHV-1gB has a structure similar to that of a heterodimer, and amino acid sequence analysis shows that it has 2 intracellular endoproteolytic cleavage sites (RTRR/S and RSRR/S), so that 1 site or 2 sites therein can be cleaved, and this cleavage affects the diffusion of the virus between cells. The gB protein is encoded by 948 amino acids, contains 10 glycosylation sites at the nitrogen terminus, and contains 10 highly conserved cysteine residues in the sequence. Purified gB induces high titers of virus to neutralize antibodies in mice, and gB-expressing vaccinia virus also stimulates production of fairly high titers of virus to neutralize antibodies in rabbits. Spatz et al also induced the production of antibodies specific for gB by intramuscular injection of FHV-lgB expressing plasmids into mice. The gB protein is a well-conserved protein in the herpesviridae family, with high homology among the constituent proteins of all herpesviruses.

The gD protein is a main component of a virus envelope, exists on an infected cell membrane, has high conservation and antigenicity, can be specifically combined with molecules on the surface of cells, induces an organism to generate cellular immunity and humoral immunity, plays an important role in virus penetration into susceptible cells, and is one of main target cells of host cellular immunity and humoral immunity reaction. Horimoto et al purified about 59kDa of gD glycoprotein as hemagglutinin from FHV-1 using ConA agarose, ion exchange and gel filtration chromatography. The nucleic acid sequence analysis shows that the FHV-1 virus genome is 1125bp long, is coded by 374 amino acids and has the molecular weight of 43.2kDa. Comparison of the gD of FHV-1 with the gD gene products of other herpes viruses revealed that the 6 cysteine backbones that make up their disulfide bonds are highly conserved. Monoclonal antibodies against gD have complement independent virus neutralizing properties. In other herpes virus classes, the gD gene, although different in biological function, is a non-essential gene for viral infection in vivo and replication in vitro.

The gE protein is an important envelope glycoprotein of FHV-1, influences the release, intercellular transmission and virulence of the virus, and is used as an object for constructing a deletion marker vaccine. Meanwhile, the gE antibody in the serum becomes a reliable marker for the existence of FHV-1 infection in the immunized cat.

gC is a multifunctional glycoprotein, which, although not essential for virus propagation, plays a very important role in adsorption of virus, release of virions, determination of virus virulence, and influencing virus stability. In addition, gC is also involved in humoral immunity, cellular immunity, immune evasion mechanism of virus, and the like.

In the traditional vaccine, gB and gD proteins are adopted to prepare the vaccine, but the effect of the vaccine is general and commercialization is not realized. The invention adopts the truncated bodies of the three proteins of gC, gD and gE as new recombinant proteins, and the obtained vaccine has better effect and lower cost and is easy to realize commercial application.

Disclosure of Invention

The invention aims to provide an antigen fragment and a truncation of a recombinant protein of a feline herpesvirus type I HR-1 strain and application thereof in vaccines, wherein in the selection of target points, envelope glycoprotein gD which is very key for virus invasion into host cells, two proteins related to virus immune escape, gC and gE are selected, three target points of gD, gC and gE are selected, a structure is analyzed and tested, the three proteins are truncated and combined to obtain a recombinant protein, and a trivalent vaccine is prepared, so that high protection efficiency can be provided. The vaccine has the advantages of excellent quality, high immune effect, stable immune effect, low cost, immune protection in a short time and the like.

The technical scheme of the invention is realized as follows:

the invention provides a protein shown in the following 1), 2) or 3) or a truncated body thereof, wherein the truncated body is shown in any one of the following:

1) The 25 th to 288 th amino acids from the N end of the envelope glycoprotein gD of the feline herpesvirus vaccine type I invading host cells, the amino acid sequence of which is shown in SEQ ID NO. 1;

2) Amino acid sequences of 29 th to 487 th amino acids of a feline herpes virus vaccine type I immune escape related protein gC from an N end are shown as SEQ ID NO. 2;

3) The 20 th-365 th amino acid of the I-type immune escape related protein gE of the herpesvirus cat vaccine is from the N end, and the amino acid sequence of the gE is shown as SEQ ID NO. 3;

the protein is at least one of gD, gC and gE.

The invention further protects a gene for coding the protein shown in 1), 2) or 3), wherein the nucleotide sequence of the gene for coding 1) the envelope glycoprotein gD truncated body of the feline herpesvirus vaccine type I invading host cell is shown in SEQ ID NO. 4; the nucleotide sequence of the gene of the I-type immune escape related protein gC truncation of the encoding 2) feline herpesvirus vaccine is shown as SEQ ID No. 5; the nucleotide sequence of the gene coding 3) the I-type immune escape related protein gE truncation of the feline herpes virus vaccine is shown as SEQ ID NO. 6.

The invention further protects an expression vector comprising the gene.

The present invention further provides a host cell comprising the vector.

The invention further provides a method for preparing the protein, which comprises the step of inducing the host cell to express the protein.

As a further improvement of the invention, the expression vector is pcDNA3.1 (+); the host cell is Escherichia coli.

The invention further provides a vaccine for preventing the I-type related diseases of the feline herpesvirus vaccine, which comprises the protein and a medically acceptable carrier.

The invention further protects the application of the protein in the preparation of the feline herpesvirus vaccine type I trivalent vaccine.

The invention further provides a method of immunizing a feline comprising administering to the feline the vaccine described above.

As a further improvement of the invention, the vaccine is administered intramuscularly, intradermally, subcutaneously, orally or intranasally.

The invention further protects the application of the protein or the truncated body thereof and/or the coding gene and/or the expression vector and/or the host cell as an antigen in preparing an antibody aiming at the I type of the feline herpesvirus vaccine;

or, the protein or its truncated body and/or the coding gene and/or the expression vector and/or the host cell in the preparation of products for preventing and/or treating diseases caused by feline herpesvirus vaccine type I;

or the use of the above protein or a truncation thereof and/or the above coding gene and/or the above expression vector and/or the above host cell for the prevention and/or treatment of a disease caused by feline herpesvirus vaccine type I.

The invention further provides the use of a protein as defined above or a truncation thereof and/or a gene encoding as defined above and/or an expression vector as defined above and/or a host cell as defined above in any one of the following a 1) to a 6):

a1 Inhibit viral infection;

a2 Preparing a product for inhibiting viral infection;

a3 Inhibit binding of the virus to the host cell;

a4 Preparing a product that inhibits binding of the virus to the host cell;

a5 Inhibit viral entry;

a6 Preparing a product for inhibiting virus invasion;

or, the virus is a feline herpesvirus.

The invention further provides a product, the active ingredient of which is the protein or the truncated body thereof;

the product has the function of any one of the following b 1) -b 3):

b1 Inhibiting viral infection;

b2 Inhibit binding of the virus to the host cell;

b3 Inhibit viral entry;

or, the product is a medicament or vaccine;

or, the virus is a feline herpesvirus.

The invention further protects a polyclonal antibody which is prepared by taking the protein or the truncated body thereof as immunogen.

The invention has the following beneficial effects: according to the feline herpesvirus vaccine, key envelope glycoprotein gD related to virus invasion host cells, two proteins related to virus immune escape, gC and gE, and three targets of gD, gC and gE are selected to prepare a trivalent vaccine, so that on one hand, an antibody for blocking virus invasion into host cells is generated, on the other hand, an antibody for preventing virus escape from immune system attack is generated, and therefore a very high-efficient vaccine protection efficiency can be provided.

Drawings

In order to more clearly illustrate the embodiments of the present invention or the technical solutions in the prior art, the drawings used in the description of the embodiments or the prior art will be briefly described below, and it is obvious that the drawings in the following description are only some embodiments of the present invention, and for those skilled in the art, other drawings can be obtained according to these drawings without creative efforts.

FIG. 1 is a diagram of a pcDNA3.1 (+) -FHV-1 _gD-translation-8 XHis (1) vector prepared in example 1 of the present invention;

FIG. 2 is a diagram of pcDNA3.1 (+) -FHV-1 \ u gC-translation-8 XHis (1) vector prepared in example 1 of the present invention

FIG. 3 is a drawing of a pcDNA3.1 (+) -FHV-1 ugE-transcription-8 XHis (1) vector prepared in example 1 of the present invention;

FIG. 4 is an SDS-PAGE pattern of recombinant gD, gC and gE proteins in example 2 of the present invention;

FIG. 5 is a graph showing the weight change of kittens in each group in example 5 of the present invention;

fig. 6 is a graph of body temperature changes for various groups of kittens in example 5 of the present invention.

Detailed Description

The technical solutions in the embodiments of the present invention will be described clearly and completely below, and it is obvious that the described embodiments are only a part of the embodiments of the present invention, and not all of the embodiments. All other embodiments, which can be derived by a person skilled in the art from the embodiments given herein without making any creative effort, shall fall within the protection scope of the present invention.

Example 1 construction of gD, gC and gE protein expression vectors

The protein comprises the following proteins shown in 1), 2) or 3) or a truncated body thereof, wherein the truncated body is shown in any one of the following formulas:

1) 25-288 amino acids from the N end of envelope glycoprotein gD of feline herpes virus vaccine I invading host cells, and the amino acid sequence is shown as SEQ ID NO. 1;

the protein is at least one of gD, gC and gE.

The invention uses the escherichia coli as an expression system, in order to obtain higher expression efficiency and higher expression quantity, codon optimization is carried out during the expression of the exogenous protein, and the exogenous protein is reversely translated into nucleotide sequences, and the obtained nucleotide sequences are respectively:

the nucleotide sequence of the gene for coding 1) the envelope glycoprotein gD truncated body of the feline herpesvirus vaccine type I invading host cell is shown as SEQ ID NO. 4;

the nucleotide sequence of the gene of the type I immune escape related protein gC truncation of the encoding 2) feline herpes virus vaccine is shown as SEQ ID NO. 5;

the nucleotide sequence of the gene coding 3) the I-type immune escape related protein gE truncation of the feline herpes virus vaccine is shown as SEQ ID NO. 6.

The gene sequence was synthesized by Guangzhou Aiji Biotechnology, inc. and ligated to a vector named: pCDNA3.1 (+), 5428bp in size, resistance: amp, insertion site: 5' end: ecoRI;3' end: xabi, to obtain recombinant plasmids of gD, gC and gE, respectively.

The obtained pcDNA3.1 (+) -FHV-1 _gD-translation-8 xHis (1) has the size of 6223bp, and the vector diagram is shown in figure 1;

the resulting pcDNA3.1 (+) -FHV-1 uggC-translation-8 XHis (1) has a size of 6808bp and the vector map is shown in FIG. 2;

the resulting pcDNA3.1 (+) -FHV-1 ugE-translation-8 XHis (1) has a size of 6460bp and the vector map is shown in FIG. 3.

EXAMPLE 2 expression and purification of recombinant proteins

The three recombinant expression vectors prepared in example 1 were transformed into E.coli DH 5. Alpha. Respectively, spread on LB plates containing ampicillin (final concentration 100. Mu.g/mL), and cultured overnight at 37 ℃. Single colonies were picked and inoculated into 100mL LB medium containing ampicillin (final concentration 100. Mu.g/mL), at 37 ℃ at 220r/min, and cultured overnight. Centrifuging at 7000r/min for 3min, collecting thallus, and extracting plasmid with Tiangen large-scale plasmid extraction kit. The obtained plasmid is filtered and sterilized at 0.22 mu m, and the concentration of the plasmid is measured by a nano-drop nucleic acid detector. Storing at-20 deg.C for use.

300 mu g of target plasmid and 1.2mL of 0.5mg/mL PEI are respectively added into 3750 mu L of OTM to be mixed by turbine oscillation for 3s, the mixture is mixed after standing for 10min, and the mixture is kept standing for 10min after being mixed by turbine oscillation for 3 s. After standing, the liquid was added to 300mL of a solution having a cell density of 1X 10 ⁶ The HEK293s suspension cells were cultured at 37 ℃ and 120r/min with 5% carbon dioxide for 48 hours. The culture was centrifuged at 3000r/min for 5min to collect the cells, and stored at-80 ℃.

Cells were disrupted with 50mL Buffer (500 mM Tris-HCl,0.2M NaCl, pH = 8.0); carrying out 175W ultrasonic crushing for 3s at an interval of 4s for 45min; finally, centrifuging for 30min at 4 ℃ and 10000r/min of rotation speed, and collecting the supernatant. Separating the supernatant with Ni column, eluting with gradient imidazole solution, and detecting the content of the target protein in the eluate by SDS-PAGE electrophoresis (FIG. 4). The eluate containing the target protein is subjected to concentration dialysis by using a 10kDa ultrafiltration tube, a 10kDa dialysis bag and a PBS solution with pH = 7.4. Concentrating to obtain gD, gC and gE target proteins, filtering and sterilizing through a 0.22 mu m filter membrane, and storing at-20 ℃ for later use.

Example 3 formulation of trivalent vaccine type I feline herpesvirus vaccine at different concentrations

The purified gD, gC and gE were mixed at a protein mass ratio of 1. Meanwhile, protein mixtures without gD protein (control 1), gC protein (control 2) and gE protein (control 3) were prepared as controls.

ISA 201 VG adjuvant: the ISA 201 VG adjuvant is input into an emulsification tank, and the prepared protein mixed solution with the same amount (W: W) is slowly input (the flow rate is 5-6L/min) under the stirring condition (200 r/min). Respectively adding different protein mixed solutions, increasing the stirring speed to 300r/min, and continuously stirring for 20-30 minutes (the temperature of the whole emulsification process is controlled at 30-32 ℃). The vessel was cooled to below 15 ℃ during stirring, the stirring was stopped and the emulsion was allowed to stand below 15 ℃ for 24 hours. Finally, 100. Mu.g/ml (test 1), 200. Mu.g/ml (test 2) and 400. Mu.g/ml (test 3) of the trivalent vaccine of feline herpesvirus vaccine type I and 3 control groups were obtained.

Example 4 serum antibody content and potency of feline herpesvirus type I vaccine after immunization

8 groups (table 1) are set, 5 Chinese garden cats of 2-3 months age are in each group, and the results are negative when FHV-1, FCV and FPV are detected. Peripheral blood is collected, FHV-1 antibody is detected, and pet cats (40) with negative antibody are screened out for experiment. The vaccines of the test groups 1-3 and the control groups 1-3 are injected into muscles at the dose of 0.05ml respectively, the PBS buffer solution with the same amount is injected into the negative control group, and the Miaosanduo vaccine with the same amount is injected into the positive control group. The second immunization was performed after 7d and the third immunization was performed after 14 d. All cats were bled from the jugular vein before immunization and 7, 14, and 28 days after immunization, and the serum was isolated and the change in antibody titer was determined by ELISA. Specific results are shown in table 2.

TABLE 1 vaccine groups

Grouping	Composition (I)	Dosage form
			Test group
1	100 mu g/ml feline herpesvirus vaccine type I trivalent vaccine	0.05ml
			Test group 2	Type I trivalent vaccine of feline herpesvirus vaccine 200 mug/ml	0.05ml
Test group 3	400 mug/ml feline herpesvirus vaccine type I trivalent vaccine	0.05ml
			Control group
1	Bivalent vaccine of feline herpes virus vaccine type I without addition of gD protein	0.05ml
			Control group 2	Bivalent vaccine of feline herpes virus vaccine type I without addition of gC protein	0.05ml
Control group 3	Feline herpesvirus vaccine type I bivalent vaccine without added gE protein	0.05ml
			Negative control group	PBS	0.05ml
Positive control group	Miaosan duo	0.05ml

TABLE 2 serum antibody content Change

Group of	Pre-immune	One need not	Two exempt from	Sanwu
					Test group
1	<10	1:200	1:1800	1:5400
					Test group 2	<10	1:600	1:1800	1:16200
Test group 3	<10	1:600	1:5400	1:16200
					Control group 1	<10	1:200	1:600	1:5400
Control group 2	<10	1:200	1:600	1:1800
					Control group 3	<10	1:200	1:600	1:1800
Negative control group	<10	<10	<10	<10
					Positive control group	<10	1:200	1:1800	1:5400

Example 5 clinical situation after immunization with feline herpesvirus type I vaccine

And measuring the body temperature and the body weight of the 40 immunized Chinese garden cats every 7 days from the beginning of immunization, and observing whether the ingestion, drinking and spirit of each group of immunized cats have obvious changes, systemic adverse reactions or not and whether local adverse reactions occur at the injection part or not. As shown in Table 3, no adverse symptoms appeared in each test cat batch, normal ingestion and drinking, and no adverse reactions at the injection site. Cats in each group were stable in body temperature and continued to gain body weight (fig. 5 and 6).

TABLE 3 clinical observations of the groups of test cats

Example 6 pseudovirus neutralization assay

HEK293T cells at 8X 10 ⁵ Cell/well 6-well plates, 37 ℃ C., 5% CO ₂ Incubators were incubated overnight to 90% confluence. 2 u g pNL4-3.luc.RE plasmid and 2 u g pVAX1-FHV-1 plasmid were transfected into 293T cells, transfection reagent lipofectamine3000. And after transfection for 48 hours, collecting culture supernatant, centrifuging and subpackaging to obtain the pseudovirus solution.

The 293T cells were plated 10 per well in 96-well plates ⁴ And (3) mixing 10 mu L of normal saline, the vaccines prepared by the test groups 1-3 and the control groups 1-3 and the 'Miaosan' vaccine of the positive control group with 10 mu L of pseudovirus solution in 1mL of DMEM medium respectively when the cell grows to 90% fusion degree by the next day, incubating for 2h at 37 ℃, and replacing the mixed solution with the 96-well cell medium. Each serum group was plated with 5 replicate wells at 37 ℃ 5% CO ₂ The incubator is used for 24h. After replacing with a new DMEM medium containing 10% FBS and continuing the culture for 48 hours, the luminescence values of each group were measured to calculate the pseudoviral infection inhibition rate, and the results are shown in Table 2. The vaccines prepared by the test groups 3-5 of the invention have better inhibition rate.

TABLE 4 false virus inhibition ratio of each group of vaccines

Example 7 challenge assay to evaluate the efficacy of feline herpesvirus type I vaccines

(1) Clinical changes after FHV-1 virus challenge

After the first immunization 42d, use 10 ⁸ TCID ₅₀ the/mL feline herpes FHV-1 virus is used for combating poison of cats in each experimental group, and the change of ingestion, drinking water, body temperature and clinical symptoms of each group of immunized cats is observed for 14 days continuously. Cats were scored according to Table 5 for clinical symptoms, and the status of each symptom was counted and the final score was calculated (Table 6). As can be seen from Table 6, the vaccine for feline herpesvirus type I achieves complete protection at an immunizing dose of more than 200 mug/ml, and the vaccine is safe.

TABLE 5 clinical scoring method after FHV-1 challenge

TABLE 6 clinical symptoms and scores in post-FHV-1 challenge trial group 1

TABLE 7 clinical symptoms and scores in post-FHV-1 challenge test group 2

TABLE 8 clinical symptoms and scores in post-FHV-1 challenge trial group 3

TABLE 9 clinical symptoms and scores of control group 1 after FHV-1 challenge

TABLE 10 clinical symptoms and scores of control group 2 after FHV-1 challenge

TABLE 11 clinical symptoms and scores of control group 3 after FHV-1 challenge

TABLE 12 clinical symptoms and scores of negative control group after FHV-1 challenge

TABLE 13 clinical symptoms and scores of post-FHV-1 challenge positive control group

(2) Respiratory tract viral load after FHV-1 virus challenge

14 days after challenge, nasal and pharyngeal swabs from all cats were collected for FHV-1 qPCR detection. Firstly, the concentration of the FHV-1 standard substance is measured to be 8.30 multiplied by 10 ¹⁰ copy/. Mu.L, after dilution in a gradient, the samples were positive and negative according to the standard curve they showed. The results are shown in Table 14. The inventionThe vaccines of test groups 2 and 3 have high protective efficiency.

TABLE 14 FHV-1 challenge all Cat cases

The above description is only for the purpose of illustrating the preferred embodiments of the present invention and is not to be construed as limiting the invention, and any modifications, equivalents, improvements and the like that fall within the spirit and principle of the present invention are intended to be included therein.

Claims

1. A protein represented by 1), 2) or 3) below or a truncation thereof, wherein the truncation is any one of the following:

1) The envelope glycoprotein gD of the feline herpes virus type I invading host cells starts from the 25 th to the 288 th amino acids from the N end, and the amino acid sequence is shown as SEQ ID NO. 1;

2) Amino acid sequences of 29 th to 487 th amino acids of a feline herpes virus type I immune escape related protein gC from an N end are shown in SEQ ID NO. 2;

3) Amino acid of 20 th-365 th site of feline herpes virus type I immune escape related protein gE from the N end, and the amino acid sequence is shown as SEQ ID NO. 3;

the protein is at least one of gD, gC and gE.

2. A gene encoding the protein of claim 1), 2) or 3), wherein the nucleotide sequence of the gene encoding 1) the gdd truncation of the envelope glycoprotein of a feline herpesvirus vaccine type I invading host cells is shown in SEQ ID No. 4; the nucleotide sequence of the gene coding 2) feline herpes virus type I immune escape related protein gC truncation is shown in SEQ ID NO. 5; the nucleotide sequence of the gene of the gE truncated body of the type I immune escape related protein of the code 3) feline herpes virus is shown as SEQ ID NO. 6.

3. An expression vector comprising the gene of claim 2.

4. A host cell comprising the vector of claim 3.

5. A method for producing the protein of claim 1, comprising the step of inducing the host cell of claim 4 to express the protein.

6. The method of claim 5, wherein the expression vector is pcDNA3.1 (+); the host cell is Escherichia coli.

7. A vaccine for preventing a feline herpesvirus vaccine type I related disease comprising the protein of claim 1 and a pharmaceutically acceptable carrier.

8. Use of a protein according to claim 1 or a truncation thereof and/or a gene encoding the same according to claim 2 and/or an expression vector according to claim 3 and/or a host cell according to claim 4 as an antigen in the preparation of an antibody against feline herpesvirus vaccine type I;

or, the use of the protein or its truncation according to claim 1 and/or the coding gene according to claim 2 and/or the expression vector according to claim 3 and/or the host cell according to claim 4 for the preparation of a product for the prophylaxis and/or treatment of diseases caused by feline herpesvirus vaccine type I;

or, the use of the protein or its truncation according to claim 1 and/or the coding gene according to claim 2 and/or the expression vector according to claim 3 and/or the host cell according to claim 4 for the prophylaxis and/or treatment of diseases caused by feline herpesvirus vaccine type I.

9. Use of the protein of claim 1 or a truncation thereof and/or the coding gene of claim 2 and/or the expression vector of claim 3 and/or the host cell of claim 4 in any one of a 1) to a 6) below:

a1 Inhibit viral infection;

a2 Preparing a product for inhibiting viral infection;

a3 Inhibit binding of the virus to the host cell;

a4 Preparing a product that inhibits binding of the virus to the host cell;

a5 Inhibit virus entry;

a6 Preparing a product that inhibits viral entry;

or, the virus is a feline herpesvirus.

10. A product comprising, as an active ingredient, the protein of claim 1 or a truncation thereof;

the product has the function of any one of the following b 1) -b 3):

b1 Inhibit viral infection;

b2 Inhibit binding of the virus to the host cell;

b3 Inhibit viral entry;

or, the product is a medicament or vaccine;

or, the virus is a feline herpesvirus.

11. A polyclonal antibody prepared by using the protein or its truncated form of claim 1 as an immunogen.