CN105294840B - A kind of peptide fragment for preventing and treating the infection of intestines pathogenic escherichia coli - Google Patents
A kind of peptide fragment for preventing and treating the infection of intestines pathogenic escherichia coli Download PDFInfo
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- CN105294840B CN105294840B CN201510811930.XA CN201510811930A CN105294840B CN 105294840 B CN105294840 B CN 105294840B CN 201510811930 A CN201510811930 A CN 201510811930A CN 105294840 B CN105294840 B CN 105294840B
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- escherichia coli
- pathogenic escherichia
- infection
- espb
- epec
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- Y—GENERAL TAGGING OF NEW TECHNOLOGICAL DEVELOPMENTS; GENERAL TAGGING OF CROSS-SECTIONAL TECHNOLOGIES SPANNING OVER SEVERAL SECTIONS OF THE IPC; TECHNICAL SUBJECTS COVERED BY FORMER USPC CROSS-REFERENCE ART COLLECTIONS [XRACs] AND DIGESTS
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- Y02A—TECHNOLOGIES FOR ADAPTATION TO CLIMATE CHANGE
- Y02A50/00—TECHNOLOGIES FOR ADAPTATION TO CLIMATE CHANGE in human health protection, e.g. against extreme weather
- Y02A50/30—Against vector-borne diseases, e.g. mosquito-borne, fly-borne, tick-borne or waterborne diseases whose impact is exacerbated by climate change
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Abstract
The present invention provides a kind of polypeptides for preventing and treating the infection of intestines pathogenic escherichia coli comprising SEQ ID NO：1、SEQ ID NO：2、SEQ ID NO：3 or SEQ ID NO：4 amino acid sequence.Technical solution using the present invention, the affinity for the polypeptide and EspB albumen that prevent and treat the infection of intestines pathogenic escherichia coli is higher than reference protein, can be used for preventing and treating the polypeptide of intestines pathogenic escherichia coli infection can inhibit the adherency of EPEC and 2 cells of HEp, block the function of EspB, to reduce absorption of the EPEC to epithelial cell, new direction is provided for EPEC treatments, the drug for research and development prevention and treatment EPEC is laid a good foundation.
Description
Technical field
The invention belongs to biotechnology more particularly to it is a kind of for prevent and treat intestines pathogenic escherichia coli infection
Peptide fragment.
Background technology
Broad-spectrum antibiotic therapy is all made of for the treatment of enteropathogenic E.Coli at present, no specificity is thin for such
The inhibitor of bacterium.Using antibiosis extract for treating, drug resistance is easy tod produce, Resistance mutation bacterium is made to assemble in human body, gives later sense
It is next difficult to contaminate treatment zone.
Epec, enteropathogenic e.coli (enteropathogenic E.coli, EPEC) is to cause global infantile diarrhea
One of with the important pathogen of adult sporadic diarrhea, current study show that EPEC mainly passes through damage of sticking and fall off
(attaching and effacing injury, A/E injury, i.e. A/E damage) leads to intestinal mucosal injury.Intestines are pathogenic big
The characteristics of uncommon bacterium EPEC of intestines angstrom infects is that pathogen energy instinct adheres to host cell membrane, destroys cell microvillus, and viscous
Induction forms cup sample basilar memebrane by cytoskeleton albumen under attached bacteria, this phenomenon referred to as " adhere to and the damage that falls off ".EPEC
Adherency and drop out effects be characterized in relying on EspB, EspD and EspA transport protein and constitute tight adhesion to host cell,
And the scavenger-cell microvillus under adherent cell, accumulate filamentous actin.EspB albumen can with EspD protein-interactings and
Insertion Into Host Cell film forms micropore so that it is thin that EPEC virulence factors can be directly entered host by the micropore formed on cell membrane
The virulence factor of born of the same parents, invasion promote bacterial adhesion and smooth out the formation of effect.The mutation EPEC of EspB missings, which cannot be mediated, to be closed on
The extension of adherent cell microvillus can not prevent the phagocytosis of macrophage.Since EspB albumen is the pathogenic large intestine of intestines
The pathogenic key protein of bacillus will find new plan if the substance for the pathogenic effects that can inhibit EPEC can be found for EPEC treatments
Slightly, major contribution is made for the following prevention and treatment EPEC.
Invention content
For the above technical problem, the invention discloses a kind of peptides for preventing and treating the infection of intestines pathogenic escherichia coli
Section, it was demonstrated that the pathogenic effects of EPEC can be inhibited, can targeting block EPEC it is pathogenic, for research and development prevention and treatment EPEC medicine
Object is laid a good foundation.
In this regard, the technical solution adopted by the present invention is：
A kind of polypeptide for preventing and treating the infection of intestines pathogenic escherichia coli, by SEQ ID NO：1、SEQ ID NO：
2, SEQ ID NO：3 or SEQ ID NO：4 amino acid sequence composition.
The present invention also provides the nucleic acid molecules for encoding polypeptide as described above.
The present invention also provides the expression cassette containing the nucleic acid molecules, recombinant vector, transgenic cell line or recombinant bacteriums.
The present invention also provides a kind of compositions including polypeptide as described above.
It is further preferred that the composition of the polypeptide also includes bactericide.
It is further preferred that the composition of the polypeptide is also included as realizing that the function except bactericidal is added with acting on
Non-polypeptide ingredient.
The present invention also provides polypeptide as described above, nucleic acid molecules as described above or compositions as described above to make
Purposes in standby drug, for killing or inhibiting epec, enteropathogenic e.coli.
Compared with prior art, beneficial effects of the present invention are：
Technical solution using the present invention, the polypeptide and EspB for preventing and treating the infection of intestines pathogenic escherichia coli
The affinity of albumen is higher than reference protein, and in vitro study is shown, for preventing and treating the more of intestines pathogenic escherichia coli infection
Peptide can inhibit the adherency of EPEC and HEp-2 cells, block the function of EspB, to reduce absorption of the EPEC to epithelial cell,
New direction is provided for EPEC treatments, the drug for research and development prevention and treatment EPEC is laid a good foundation.
Description of the drawings
Fig. 1 is that the present invention detects EspB protein expression figures using Western Blot methods.In figure, A is structure
PET21b-EspB expression plasmids are transfected into the expression figure after escherichia coli, and the anti-human 6- histidines monoclonal antibody of mouse is
Main antibody, 1 for EspB expression vectors transfection bacterial lysates, 2 for culture supernatant expression recombination EspB albumen, 1 and 2 point
The bacterial lysates and culture supernatant expression recombination EspB albumen situations of the transfection of EspB expression vectors are not shown.B is purifying
EspB protein expression figures.
Fig. 2 is 12 kinds of positive bacteriophages screened and vcsM13 control of the invention and EspB and 6- histidines small peptide parent
With the qualification figure of power size ELISA method, each experiment is repeated 3 times above, takes its mean as final analysis data.
Specific implementation mode
Below in conjunction with the accompanying drawings, technical scheme of the present invention is described in further detail.
1. vivoexpression EspB albumen；
From E2348/69 (O127：H6) bacterial strain expands EspB segments, inserts this genetic fragment using standard molecular methods
Enter the sites pET21b expression vector BamHI and EcoRI, to one pET21b- for containing 6 (His) histidine stumps of structure
EspB expression vectors.Induce the recombination large intestine angstrom of pET21b-EspB expression vectors transfection uncommon by the way that IPTG is added into culture medium
Bacterium expresses EspB albumen.Cell is collected by centrifugation after the IPTG of 1mM is added, it is described using Qiagen companies A buffer solution suspension cells
A buffer solutions are 20mM Tris, the 500mM NaCl, pH 9 of A buffer solutions production.Cell is hanged after sound wave cracking process lytic cell
Liquid is centrifuged, and is collected supernatant and is used for Ni2+Exchange membrane (Qiagen companies) filters.EspB albumen containing His labels is eluted
Liquid (Qiagen companies) elutes, and albumen is collected using the anti-His monoclonal antibodies Western blot methods analysis of mouse.
His-EspB albumen concentration is recombinated in Bradford methods (Bio-Rad, Hercules, CA, USA) quantitative collection solution, later
It is stored in -70 DEG C of refrigerator.
The screening of 2.EspB binding proteins specifics
Using 12-mer with hangar (New England BioLabs, Ipswich, MA, USA) using on bacteriophage M13-
Filter out EspB binding proteins specifics.The solution that 150 μ L are mixed with to 10 μ g/mL EspB albumen and 0.1M sodium bicarbonates is added
In sterile polystyrene Petri dish, concussion is until culture dish surface moistens completely repeatedly.It is coated with the culture of EspB albumen
Ware is washed after cleaning blocking with calf proteinemina with 0.05%PBST buffer solutions.Take 10 μ L that culture is added with the diluted stostes of PBST
Base is incubated 2h under room temperature.For coated culture dish with after being washed with 0.05%PBST, remaining adherency bacteriophage is eluted use
In amplification.After three-wheel expands, eluent is expanded in ER2738 culture mediums, purified with polyethylene glycol precipitation and according to
Reagent operation instructions are quantitative.
3.ELISA methods screen positive bacteriophage
With EspB albumen and control 6- histidine peptides 96 orifice plates of coating overnight, buffer solution is blocked to block, is added per hole
1014The phage clone or check sample of pfu is incubated 1h under room temperature；The M13 of horseradish peroxidase-labeled is added, under room temperature
It is incubated 1h；The benzidine in 50 holes μ L/ is added；The 2M H in 50 holes μ L/ are added after 20min2SO4Terminate reaction；Detection sample exists
Absorbance (A) value at 450nm wavelength.If the A values of sample consider target protein higher than control bacteriophage and peptide 2 times or more
There is higher affinity with EspB albumen.
4.DNA is sequenced and peptide chain synthesis
It is expanded with hangar according to New England BioLabs, Ipswich, MA, USA reagent operation specifications 12-mer
DNA fragmentation in positive bacteriophage, and sanger is sent to be sequenced；BioEdit sequence alignments software for editing is applied to analyze DNA sequences later
Row.Target peptide chain is synthesized by Sigma-Aldrich, and purity is more than 98%.The C of 6 histidines is short to be added to Gly-
Negative control is used as on Gly-Gly-Ser space structures.
5. cell activity assays
HEp-2 cells are with 2 × 103The density in/hole is inoculated into 96 well culture plates, is changed into containing 1% small ox blood after adherent overnight
Clear DMEM medium cultures 24 hours, then be incubated 48 hours with a series of small peptide of gradient dilutions.It is thin with the analysis of MTT decoration methods
Cytoactive, 490 nanometers light absorption values represent relative activity cell number.
6.HEp-2 cells inhibit experiment
With reference to Infect Immun.2006；74(12):6920-8；J Agric Food Chem.2013；61(11):
2748-54.J Food Prot.2008；71(11):The method that 2272-7 is introduced is inhibited using EPEC E2348/69 bacterial strains
Experiment.Before experiment, EPEC bacterial strains are incubated with 4ml sugar-free trypsase culture mediums, are cultivated later with the DMEM of 5% calf serum
Liquid and the washing of 1%SDMEM culture solutions.The EPEC cell inoculations grown on culture dish will be tiltedly draped over one's shoulders to cultivate to fresh 1%SDMEM
Base, part are adsorbed.HEp-2 cells are suspended in the Gibco culture solutions containing 10% calf serum, with 5 × 104/ hole cell density
It is inoculated into 24 well culture plates.To every 107It is respectively the short of 10,50,100, and, 200 μ g/mL that a series of concentration, which are added, in cell
Peptide；The 6 histidine oligopeptides of a concentration of 200 μ g/mL are then added in negative control group.Culture plate is in 37 DEG C of CO230 points are incubated in incubator
Clock cleans the non-attached cell of removal with PBS buffer solution later.Culture dish fixes 10 minutes with methanol, dry, using Giemsa methods
Dyeing 20 minutes, later with amplification factor be 100 × comparison micrscope under observe.It can at least be seen under this amplification factor
Observe 100 continuous HEp-2.If a cell is including 4 or 4 or more EPEC bacterium are considered that positive cell, tool are adsorbed in part
Its standby phenotypic features；Local adherent cell proportional representation adsorption rate in per continuous 100 cells.Experiment is repeated three times every time
More than, and reduction ratio is calculated using following formula.
Reduction ratio=(negative control group mean-experimental group mean)/positive controls.
7. statistical analysis
Data of analyzing and researching are used for using software GraphPad Prism v5.01.Difference between two groups is examined with T.It is more
Comparison among groups use one-way analysis of variance.P<0.05 is considered significant difference.
8. experimental result
As shown in Figure 1, the pET21b-EspB expression plasmids of structure successfully express EspB after being transfected into escherichia coli
Albumen, and Western blot method validation Protein expression and purification albumen is applied, verification result is as shown in Fig. 2, can by Fig. 2
See there is a bright band, EspB albumen to obtain high expression at 37KD.
Enrichment experiment is carried out to EspB protein binding bacteriophages, shown in 1.By table 1 as it can be seen that Ph.D.12 eggs
Propylhomoserin display technique of bacteriophage is for screening EspB binding proteins specifics, and three-wheel affinity Selection experiment is the result shows that can be special
Property combination EspB albumen bacteriophage there is enrichment phenomenon, preliminary screening, which goes out 12 clones and EspB albumen, may have knot
Cooperation is used.
Table 1EspB protein binding bacteriophage enrichment experiment results
The control of positive bacteriophage and vcsM13 and EspB the and 6- histidine small peptide affinity sizes that 12 kinds are screened
It is identified with ELISA method, each experiment is repeated 3 times above, takes its mean as final analysis data, and the results are shown in Figure 2,
From Figure 2 it can be seen that each phage clone is individually incubated with EspB albumen.
Using ELISA method Analysis and Screening go out bacteriophage peptide-6, peptide-7 to EspB albumen high-affinities,
Peptide-8 and peptide-12.According to sanger sequencing results, this four peptide section sequences are respectively：
peptide-6:YFPYSHTSPRQP；(such as SEQ ID NO：1)
peptide-7:AYKYT SALPAEA；(such as SEQ ID NO：2)
peptide-8:SLTLMNSPLGAS；(such as SEQ ID NO：3)
peptide-12:MLTLSLNPTNSA；(such as SEQ ID NO：4)
MTT experiments are carried out respectively to peptide-6, peptide-7, peptide-8 and peptide-12, MTT tests number
It is as shown in table 2 according to display.As can be seen from Table 2, peptide-6, peptide-7, peptide-8 and peptide-12 are thin to HEp-2
Born of the same parents are without overt toxicity, and result of study shows the increase with concentration, and it is thin to HEp-2 that peptide-6 can substantially reduce EPEC
The ratio of adsorption of born of the same parents, as its a concentration of 100 μ g/mL, compared with the control group, EPEC has dropped 40% to HEp-2 ratio of adsorption.
2 polypeptide of table adheres to EPEC the influence in vitro study of HEp-2 cells
Using the technical solution of the present embodiment, we use phage display technology and find the combination of EspB protein-specifics
Polypeptide, 3 wheel enrichment experiments have screened 12 kinds of small peptides, and identify 4 using ELISA method has preferable affinity with EspB,
These polypeptides can be used for treating EPEC infection.
EspA, EspB and EspD albumen of EPEC secretions can form needle point sample microcellular structure on host cell membrane, we
EspB Specific binding proteins can be selected, by combining EspB albumen, the formation of needle point sample micropore are blocked, to inhibit EPEC pairs
The absorption of host cell.
The above content is a further detailed description of the present invention in conjunction with specific preferred embodiments, and it cannot be said that
The specific implementation of the present invention is confined to these explanations.For those of ordinary skill in the art to which the present invention belongs, exist
Under the premise of not departing from present inventive concept, a number of simple deductions or replacements can also be made, all shall be regarded as belonging to the present invention's
Protection domain.
Claims (9)
1. a kind of peptide fragment for preventing and treating the infection of intestines pathogenic escherichia coli, it is characterised in that：It is SEQ ID NO：1
Amino acid sequence.
2. the nucleic acid molecules of the peptide fragment described in coding claim 1 for preventing and treating the infection of intestines pathogenic escherichia coli.
3. the expression cassette, recombinant vector, transgenic cell line containing nucleic acid molecules described in claim 2 or recombinant bacterium.
4. a kind of combination including the peptide fragment for preventing and treating the infection of intestines pathogenic escherichia coli as described in claim 1
Object.
5. according to the composition described in claim 4, it is characterised in that：It also include bactericide.
6. according to the composition described in claim 4, it is characterised in that：Also it is included as the function and work realized except bactericidal
With and add non-polypeptide ingredient.
7. as described in claim 1 for prevent and treat intestines pathogenic escherichia coli infection peptide fragment in medicine preparation
Purposes, for inhibiting intestines pathogenic escherichia coli.
8. the purposes of nucleic acid molecules as claimed in claim 2 in medicine preparation, for inhibiting intestines pathogenic escherichia coli.
9. the purposes of composition in medicine preparation as described in claim 4,5 or 6, for inhibiting intestines pathogenic escherichia coli.
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| CN201810651430.8A CN109206484B (en) | 2015-11-20 | 2015-11-20 | Peptide segment for preventing and treating enteropathogenic escherichia coli infection |
| CN201810651397.9A CN109180786B (en) | 2015-11-20 | 2015-11-20 | Peptide fragment for preventing and treating enteropathogenic escherichia coli infection |
| CN201510811930.XA CN105294840B (en) | 2015-11-20 | 2015-11-20 | A kind of peptide fragment for preventing and treating the infection of intestines pathogenic escherichia coli |
| CN201810650486.1A CN108976289B (en) | 2015-11-20 | 2015-11-20 | Peptide fragment for preventing and treating enteropathogenic escherichia coli infection |
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| CN201810651430.8A Division CN109206484B (en) | 2015-11-20 | 2015-11-20 | Peptide segment for preventing and treating enteropathogenic escherichia coli infection |
| CN201810651397.9A Division CN109180786B (en) | 2015-11-20 | 2015-11-20 | Peptide fragment for preventing and treating enteropathogenic escherichia coli infection |
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| CN1222937A (en) * | 1996-04-23 | 1999-07-14 | 不列颠哥伦比亚大学 | Pathogenic escherichia coli associated protein |
| US20020107368A1 (en) * | 2000-12-07 | 2002-08-08 | Jing-Hui Tian | Helicobacter proteins, gene sequences and uses thereof |
| GB0315022D0 (en) * | 2003-06-26 | 2003-07-30 | Chiron Srl | Virulence-associated adhesins |
| EP1692287A4 (en) * | 2003-10-31 | 2007-03-28 | Univ British Columbia | Bacterial virulence factors and uses thereof |
| US7250261B2 (en) * | 2004-05-20 | 2007-07-31 | University Of Massachusetts | EspFu nucleic acids and proteins and uses thereof |
| ES2322116B1 (en) * | 2007-03-12 | 2010-03-29 | Consejo Superior Investig. Cientificas | ANTIBODY PRODUCING MICROORGANISM, ELEMENTS REQUIRED FOR OBTAINING, ANTIBODIES AS WELL PRODUCED, THERAPEUTIC COMPOSITIONS AND THEIR APPLICATIONS. |
| SI2514436T1 (en) * | 2007-11-07 | 2018-04-30 | Genentech, Inc. | Il-22 for use in treating microbial disorders |
| US8771668B2 (en) * | 2008-04-09 | 2014-07-08 | Cornell University | Commensal bacteria as signal mediators within a mammalian host |
| CN105456300B (en) * | 2009-02-06 | 2019-07-09 | 抗菌技术,生物技术研究与发展股份有限公司 | Antibacterial bacteriophage, phage display peptide and its application method |
| EP2557163A1 (en) * | 2011-08-12 | 2013-02-13 | SymbioGruppe GmbH & Co KG | Bacterially formed microcin S, a new antimicrobial peptide, effective against pathogenic microorganisms, e.g. enterohemorrhagic Escherichia coli (EHEC) |
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| CN108976289B (en) | 2021-06-18 |
| CN109206484A (en) | 2019-01-15 |
| CN109180786B (en) | 2021-06-18 |
| CN105294840A (en) | 2016-02-03 |
| CN109206484B (en) | 2021-06-18 |
| CN108976289A (en) | 2018-12-11 |
| CN109180786A (en) | 2019-01-11 |
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