CN116143882A - Hippocampus trimarans hepcidin antibacterial peptide and application thereof - Google Patents

Hippocampus trimarans hepcidin antibacterial peptide and application thereof Download PDF

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CN116143882A
CN116143882A CN202211251360.XA CN202211251360A CN116143882A CN 116143882 A CN116143882 A CN 116143882A CN 202211251360 A CN202211251360 A CN 202211251360A CN 116143882 A CN116143882 A CN 116143882A
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hepcidin
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hippocampus
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钟声平
魏时英
李婷婷
黄国强
黄亮华
赵龙岩
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Abstract

The invention relates to the technical field of bioengineering, in particular to preparation and application of a hippocampus trimarans antibacterial peptide, and discloses a hepcidin antibacterial peptide derived from the hippocampus trimarans for the first time, and a novel hepcidin antibacterial peptide family member named HiTr_hepcidin is obtained from a hippocampus trimarans transcriptome library for the first time. And the HiTr_hepcidin_2a polypeptide fragment with broad-spectrum antibacterial activity is prepared by adopting a solid-phase chemical synthesis method. The polypeptide fragment has strong antibacterial activity on common pathogenic bacteria of aquatic animals such as vibrio parahaemolyticus, vibrio harveyi, aeromonas hydrophila and the like, and the minimum antibacterial concentration of the polypeptide fragment on the vibrio parahaemolyticus, the vibrio harveyi and the aeromonas hydrophila is 1.5-3 mu M. Has stronger inhibiting and killing activity to common food-borne pathogenic bacteria.

Description

Hippocampus trimarans hepcidin antibacterial peptide and application thereof
Technical Field
The invention belongs to the technical field of bioengineering, and particularly relates to a Hippocampus trimaran antibacterial peptide and application thereof.
Background
Hippocampus (school name: hippocampus trimaculatus) is a small-sized teleosts belonging to the genus Hippocampus of the family Syngnathidae, and is described in Chinese pharmacopoeia (2020 edition), and has effects of warming kidney, supporting yang, resolving hard mass, and relieving swelling. Modern pharmacological studies show that Hippocampus has pharmacological activities such as anti-tumor, antithrombotic, antifatigue and antiaging. The establishment of a natural protection area of the three-spot sea horse, the establishment of a living body resource library of the three-spot sea horse and the development of a full-artificial breeding technology of the three-spot sea horse are important measures for guaranteeing sustainable utilization of germplasm resources of the three-spot sea horse.
At present, the full artificial breeding technology of the three-spot sea horses is not completely broken through, particularly, the survival rate of the three-spot sea horses is low, and the sustainable development of the artificial breeding industry of the three-spot sea horses is limited. The young fish of marine fish is easy to be infected by pathogenic bacteria such as Vibrio harveyi, mermaid luminous bacillus and the like in bait or culture water body because immune organs are not fully developed, so that the young fish of marine fish is dead in a large scale. The three-spot sea horse fish stage is also easy to be infected by pathogenic bacteria such as vibrio and the like, so that the seedling raising is failed. The antibacterial peptide (antimicrobial peptides, AMPs) is taken as an important component of the immune system of marine fish, can be taken as an antibacterial active substance to directly inhibit and kill disease microorganisms, can be taken as an immune effector molecule to coordinate a host immune defense system, and is an important immune defense mechanism of marine vertebrates such as marine fish for resisting invasion of the disease microorganisms. To date, antibacterial peptides found and identified in marine fish are mainly classified into 3 structural types, namely, antibacterial peptides with alpha helical structures, including toxalbumin (piscidin) and cynoglossus panther toxin (pardaxin) and the like; secondly, antibacterial peptides with beta-sheet structure, including defensins (defensins), hepcidins (hepcidins), liver expressed antibacterial peptides (lever-expressed an-timicrobial peptide, LEAP) and the like; and thirdly, histone-like antibacterial peptides, including histone polypeptide HLP, salmon antibacterial peptide SAM and the like. However, no studies have been reported in which antibacterial peptides have been found and identified in the hippocampus trimaculum.
Hepcidin (hepcidin) is a cationic polypeptide specifically expressed in animal livers and has important regulatory effects in both innate immunity and iron metabolism in animals, and has broad-spectrum antibacterial activity, can inhibit and kill gram-negative bacteria, gram-positive bacteria and fungi, and also has antiviral, antiparasitic and immunomodulatory biological activities. The artificially synthesized and biosynthesized hepcidin antibacterial peptide has good heat stability and water solubility, almost does not generate drug resistance, is a novel biosafety antibiotic, can replace the traditional antibiotic in marine fish seedling production to directly inhibit and kill disease organisms, can enhance the immunity of the fries, and can improve the metamorphosis survival rate of the fries.
Disclosure of Invention
In view of the above, the application provides a HiTr_hepcidin antibacterial peptide which can be used as an ecological safety antibacterial additive in aquaculture and has wide application prospect.
In order to achieve the above purpose, the technical scheme adopted by the invention is as follows:
the invention provides a Hippocampus trimaran HiTr_hepcidin antibacterial peptide, the amino acid sequence of which is shown as SEQ ID NO. 1; the method comprises the following steps:
MMKPFSLSVAVIIMLAFLFIQEGSTISLENREPDQHMVEARDDAAAEIPMDLWKVADNKRQKRHSGPCKFCCNCCGRVNFCGLCCEWRF。
another object of the present invention is to provide a HiTr_hepcidin_2a antimicrobial peptide of Hippocampus trimarans, which is a polypeptide fragment selected from HiTr_hepcidin antimicrobial peptides having antimicrobial activity, and which can form an amphipathic alpha helix structure with 2 positive charges, named: hiTr_hepcidin_2a. The amino acid sequence is SEQ ID NO.2; the method comprises the following steps:
GPCKFCCNCCGRVNFCGLCC。
the use of the above-described hippocampal HiTr_hepcidin_2a antimicrobial peptides is also within the scope of the invention, including: is used as an antibacterial additive in the aquaculture industry.
A polypeptide or protein comprising the above-described antimicrobial peptide is also within the scope of the present invention.
The invention has the following beneficial effects:
the invention provides a hepcidin antibacterial peptide family member with broad-spectrum antibacterial activity from Hippocampus trimarans for the first time, the antibacterial peptide active fragment can be prepared in a large amount through solid-phase chemical synthesis, and the polypeptide fragment has strong antibacterial effect on common pathogenic bacteria of aquatic animals such as vibrio harveyi and aeromonas hydrophila, has strong inhibitory activity on food-borne pathogenic bacteria such as staphylococcus aureus and pseudomonas fluorescens, and has antibacterial concentration and bactericidal concentration of about 3 mu M and 12 mu M for pseudomonas fluorescens. Can also be used as an ecological and safe antibacterial additive in aquaculture, and has wide application prospect.
Drawings
FIG. 1 is a diagram of the tertiary protein structure of the mature peptide of the HiTr_hepcidin antibacterial peptide;
FIG. 2 is a schematic diagram of the amphipathic alpha helix structure of the HiTr_hepcidin_2a antimicrobial peptide; in the figure, the dark black ground color represents hydrophilic amino acid, the light white ground color represents hydrophobic amino acid, and the direction indicated by the arrow is a hydrophobic surface of an alpha helical structure;
FIG. 3 is a photograph of a culture dish of HiTr_hepcidin_2a antimicrobial peptide against Aeromonas hydrophila.
Detailed Description
In order that the above objects, features and advantages of the invention will be readily understood, a more particular description of the invention will be rendered by reference to the appended drawings. In the following description, numerous specific details are set forth in order to provide a thorough understanding of the present invention. The invention may be embodied in many other forms than described herein and similarly modified by those skilled in the art without departing from the spirit or scope of the invention, which is therefore not limited to the specific embodiments disclosed below.
Example 1:
acquisition of the hippocampus trimacum HiTr_hepcidin antibacterial peptide Gene sequence:
collecting tissues such as head kidney, intestine, gill and muscle of Hippocampus trimarans, respectively extracting total RNA from the tissues, performing transcriptome library sequencing after quality inspection is qualified, completing assembly of reference transcripts of the Hippocampus trimarans by using trinity software, and finally screening full-length cDNA sequences of HiTr_hepcidin antibacterial peptide genes of the Hippocampus trimarans by using blastp software in a homologous alignment mode for the first time, wherein the full-length cDNA sequences of the genes are as follows:
ATGATGAAGCCCTTCAGTTTGTCTGTTGCAGTGATCATCATGCTTGCCTTCCTTTTTATTCAGGAGGGTTCCACCATCTCTCTTGAGAATAGGGAGCCTGACCAGCATATGGTGGAAGCCAGAGATGACGCAGCTGCTGAGATCCCAATGGACTTATGGAAGGTGGCAGACAACAAGAGGCAGAAACGCCATAGTGGACCTTGCAAATTTTGCTGCAACTGCTGCGGTCGTGTGAATTTCTGTGGCCTGTGCTGCGAATGGAGATTCTAA。
the full-length cDNA of the HiTr_hepcidin antibacterial peptide gene is translated into an amino acid sequence, and the full-length amino acid sequence of the HiTr_hepcidin antibacterial peptide is SEQ ID NO.1, which is specifically as follows:
MMKPFSLSVAVIIMLAFLFIQEGSTISLENREPDQHMVEARDDAAAEIPMDLWKVADNKRQKRHSGPCKFCCNCCGRVNFCGLCCEWRF。
example 2:
obtaining the tertiary protein structure of the mature peptide and the polypeptide fragment with antibacterial activity:
signal and mature peptides of HiTr_hepcidin antibacterial peptides were predicted using SignalP-6.0 software and utilizedhttps://aps.unmc.edu/Andhttps://swissmodel.expasy.org/websites predict physicochemical properties and tertiary structure of mature peptides, respectively.
The results show that the mature peptide consists of 30 amino acids and has a molecular formula of C 147 H 229 N 48 O 37 S 8 The molecular weight is 3542.25 daltons. The mature peptide has 5.25 positive charges and is a cationic antibacterial peptide. The tertiary structure of the protein is shown in FIG. 1 and comprises 2 beta sheets.
By means ofhttp://www.camp.bicnirrh.res.in/predict_c/The website predicts the polypeptide fragment with antibacterial activity of the mature peptide, obtains the polypeptide fragment with the length of 20 amino acids and is named as HiTr_hepcidin_2a, and the amino acid sequence of the polypeptide fragment is SEQ ID NO.2; the method comprises the following steps:
GPCKFCCNCCGRVNFCGLCC。
by means ofhttps://heliquest.ipmc.cnrs.fr/cgi-bin/ComputParams.pyThe website predicts the physical and chemical properties and structural features of HiTr_hepcidin_2a.
The result shows that the antibacterial peptide can form an amphipathic alpha-helical structure, as shown in figure 2, has obvious hydrophobic surface and hydrophilic surface, and has 2 positive charges, and is an alpha-helical cationic antibacterial peptide.
Example 3:
preparation of hippocampal HiTr_hepcidin_2a antibacterial peptide:
the amino acid sequence of the HiTr-hepcidin-2 a antibacterial peptide is submitted to Hubei blazing biotechnology Co-Ltd, and the HiTr-hepcidin-2 a antibacterial peptide crude product is synthesized by the company through a solid phase chemical synthesis method, is purified through high performance liquid chromatography, is concentrated through a freeze dryer, is subjected to mass spectrum identification through a mass spectrometer, and is prepared to obtain the high-purity HiTr-hepcidin-2 a antibacterial peptide after the identification is qualified.
Example 4:
determination of antibacterial Activity of HiTr_hepcidin_2a of Hippocampus trimacum:
in this example, strains such as Escherichia coli (Escherichia coli), bacillus subtilis (Bacillus subtilis), staphylococcus aureus (Staphylococcus aureus), pseudomonas aeruginosa (Pseudomonas aeruginosa), corynebacterium glutamicum (Corynebacterium glutamicum), vibrio alginolyticus (Vibrio alginolyticus), micrococcus luteus (Micrococcus luteus), pseudomonas fluorescens (Psdeuomdafuroernnet), micrococcus solvolens (Micrococcus lysodeikticus Fleming), shigella flexneri (Shigella flexneri), vibrio parahaemolyticus (Vibrio Parahaemolyticus), vibrio harveyi (Vibrio harveyi), aeromonas hydrophila (Aeromonas hydrophila), and Prominobacter mermairei (Photobacterium damselae) were used as test strains for the antibacterial activity test. Wherein the strains are all purchased from the China academy of sciences of microbiological culture Collection center.
The method for measuring the antibacterial activity is as follows:
(1) Activation of the refrigerated strains: streaking bacterial strain (i.e. the above test strain) stored at-80deg.C on LB plate, culturing at 28deg.C (marine bacteria) or 37deg.C (non-marine bacteria) for 24 hr, picking single colony into 10mL sterile LB liquid medium, shake culturing at 28deg.C or 37deg.C and 180rpm/min for 12 hr;
(2) Preparation of bacterial suspensions: streaking a small amount of activated bacterial liquid on an MHA flat plate, culturing for 12 hours in an inverted mode, picking 1 single colony from the flat plate, streaking on an MHA slant culture medium, culturing for 12 hours at 28 ℃, eluting the slant culture by using NaPB (10 mM), measuring the OD value of the eluent by using an enzyme-labeling instrument, and adding a certain amount of eluent into the NaPB or a working culture medium to ensure that the OD value of the final bacterial suspension is 0.0018;
(3) Preparation of HiTr_hepcidin_2a antibacterial peptide working solution: filtering HiTr_hepcidin_2a antibacterial peptide with 0.22 μm filter membrane, determining protein concentration by Bradford method, diluting working solution with 1.5, 3.0, 6.0, 12, 24, 48 and 96 μm protein concentration by multiple ratio, and preserving at 4deg.C for use;
(4) Determination of minimum inhibitory concentration (MIC, minimum inhibition concentration): designing an experiment group, a blank control group and a negative control group for experiments, wherein the concentration of each antibacterial peptide is set to be 3 in parallel; the experimental results were observed by culturing in 96-well cell culture plates for 24 hours.
Wherein, each group of the reagents is as follows:
experimental group: 50. Mu.L of antibacterial peptide working solution+50. Mu.L of bacterial suspension;
blank control: 50. Mu.L of sterile water+50. Mu.L of bacterial suspension;
negative control: 50. Mu.L of working medium+50. Mu.L of the minimum concentration of the antimicrobial peptide working fluid.
(5) Determination of minimum bactericidal concentration (MBC, minimumbactericidal concentration): mu.L of the mixed culture was aspirated from each well of the cell culture plate after incubation, and the mixture was dropped onto a MHA plate and cultured for 24 hours (culture temperature of non-marine bacteria was 37℃and culture temperature of marine bacteria was 28 ℃), and colony formation was observed.
The specific test results are shown in table 1:
table 1 HiTr_hepcidin_2a antibacterial peptide antibacterial Activity determination results
Figure SMS_1
The result shows that the HiTr_hepcidin_2a antibacterial peptide has strong antibacterial activity on common pathogenic bacteria in aquaculture, wherein the minimum antibacterial concentration on vibrio parahaemolyticus, vibrio harveyi and aeromonas hydrophila is 1.5-3 mu M; the microbial agent also has stronger inhibiting and killing activity on common food-borne pathogenic bacteria, wherein the minimum inhibitory concentration on pseudomonas fluorescens is 1.5-3 mu M, and the minimum bactericidal concentration is 6-12 mu M.
Taking aeromonas hydrophila as an example in the plate culture condition of the test strain, the photo of a culture dish of the aeromonas hydrophila is shown as figure 3, the plate is divided into 7 fan-shaped areas with the same area size, and the concentration of the antibacterial peptide working solution in each area is as follows: the concentrations of the antimicrobial peptide working fluids in the different regions are marked with black letters at 1.5. Mu.M, 3.0. Mu.M, 6.0. Mu.M, 12. Mu.M, 24. Mu.M, 48. Mu.M and 96. Mu.M, and it can be seen from FIG. 3 that at concentrations of 1.5-12.0. Mu.M, the plates can grow Aeromonas hydrophila, while at concentrations of 24. Mu.M, aeromonas hydrophila cannot grow, thus indicating that the concentration of the highest antimicrobial peptide working fluid that Aeromonas hydrophila can grow is 12. Mu.M and the concentration of the lowest antimicrobial peptide working fluid that Aeromonas hydrophila can not grow when killed is 24. Mu.M. The minimum sterilization concentration of the HiTr_hepcidin_2a antibacterial peptide to aeromonas hydrophila is 12-24 mu M.
Example 5:
application of Hippocampus trimarans HiTr_hepcidin_2a antibacterial peptide in the production of Epinephelus coioides seedlings:
the embodiment provides the work of applying the antibacterial peptide as an antibacterial additive in aquaculture, and specifically comprises the following steps: preparation of HiTr_hepcidin_2a antimicrobial peptide of high purity Using the procedure described in example 3, hiTr_hepcidin_2a was prepared
The peptide is prepared into a sterilizing working solution according to the final concentration of 24 mu M, and the working solution is used for soaking the fertilized eggs of the oyster serving as an initial bait of the young garrupa for 1h, so that the aim of inhibiting and killing common pathogenic bacteria such as vibrio parahaemolyticus and vibrio harveyi in biological baits produced by raising the young garrupa is fulfilled, and the survival rate of the young garrupa is improved.
The invention discloses a hepcidin antibacterial peptide derived from Hippocampus trimarans for the first time, which is prepared from active polypeptide and subjected to antibacterial activity test, and is applied to sea fish seedling production, thereby being expected to replace traditional antibiotics to be used as a novel feed antibacterial additive with ecological safety.
The above examples merely represent a few embodiments of the present invention, which are described in more detail and are not to be construed as limiting the scope of the present invention.

Claims (6)

1. A hippocampus trimarans HiTr_hepcidin antibacterial peptide, which is characterized in that the amino acid sequence of the antibacterial peptide is SEQ ID NO.1.
2. The antimicrobial peptide of hippocampal hitr_hepcidin as set forth in claim 1, wherein the amino acid sequence of an antimicrobial active center peptide fragment of the antimicrobial peptide is shown in SEQ ID No.2, the active center peptide fragment being designated hitr_hepcidin_2a.
3. Use of the hippocampus trimara HiTr-hepcidin antibacterial peptide as claimed in claim 1 or 2 in the preparation of a bacteriostatic agent.
4. Use according to claim 3, wherein the use comprises the defense and/or elimination of microbial infections in aquaculture.
5. A polypeptide comprising the amino acid sequence of the antimicrobial peptide of claim 1.
6. A protein comprising the amino acid sequence of the antimicrobial peptide of claim 1.
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Cited By (1)

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CN116874575A (en) * 2023-08-28 2023-10-13 广西中医药大学 Apostichopus japonicus antibacterial peptide and application thereof

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* Cited by examiner, † Cited by third party
Publication number Priority date Publication date Assignee Title
CN116874575A (en) * 2023-08-28 2023-10-13 广西中医药大学 Apostichopus japonicus antibacterial peptide and application thereof
CN116874575B (en) * 2023-08-28 2024-04-19 广西中医药大学 Apostichopus japonicus antibacterial peptide and application thereof

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