Search PubMed⌕ Search

SEARCH · Search PubMed

Results for “Epitopes”

Search indexed PubMed citations on genomics, clinical trials, systematic reviews and public health. Explore titles, authors and supplied subject terms, then open the PubMed record.

Quote a phrase for an exact phrase match. Source license links do not imply unrestricted reuse.

At least 1,099 records · Page 61Linked to original sources
PubMed1987

Recognition by the human immune system of candidate vaccine epitopes of Toxoplasma gondii measured by a competitive ELISA.

A competitive ELISA for the detection of human antibody to specific candidate vaccine epitopes of Toxoplasma gondii is described. The method is based on competition between antibody in human serum and murine monoclonal antibody to bind to a crude sonicated antigen of T. gondii. A total of 301 normal human sera were tested against a panel of four anti-T. gondii murine monoclonal antibodies. The results obtained with two of the monoclonal antibodies (FMC 22 and FMC 23) gave good agreement with those of an indirect ELISA for human IgG to T. gondii, a measure of previous exposure to the parasite. The epitopes against which these two monoclonal antibodies are directed were recognized by the immune system of all patients previously exposed to the parasite, while greater than 92 and greater than 96% respectively of these patients recognized the epitopes which the other two monoclonal antibodies (FMC 18 and FMC 19) are directed against. An ELISA double antibody binding system was used to ascertain relationships in the epitope binding sites of the four monoclonal antibodies. The data obtained demonstrated that FMC 19 and FMC 22 bound to related epitopes. FMC 18, FMC 22 and FMC 23 also bound to related epitopes, but the binding of FMC 19 was found to be independent of the binding of FMC 18 and FMC 23 to their epitope binding sites.

Animals↗
PubMed1994

Epitope-specific antibody responses in market-stressed calves to bovine herpesvirus type 1.

Reciprocal competition ELISA (rcELISA) was conducted to map monoclonal antibodies (mAbs) reactive with gI, gIII and gIV glycoproteins of bovine herpesvirus type 1 (BHV-1) into epitope groups. mAbs to glycoproteins gI and gIV were divided into six epitope groups each, while gIII mAbs had been previously divided into four areas. mAbs were chosen from each epitope group to compete in cELISA wih bovine sera collected during a typical regimen of vaccination and transportation from farm to auction to feedlot. The immunodominant epitopes were identified for each BHV-1 glycoprotein. With glycoprotein gI, three epitopes defined by mAbs 1F10, D9 and 4807 were the most dominant; with glycoprotein gIII epitopes defined by mAbs G2 and 1507, and with glycoprotein gIV epitopes defined by mAbs 1102, 1106, 3C1, 3402 and 3E7 showed the maximum responses. The overall cELISA responses to each glycoprotein among two vaccination groups were also compared and it was shown that cELISA responses were significantly higher for each glycoprotein in calves receiving two vaccinations, one on the farm of origin and one at auction, than in calves receiving only one vaccination at auction.

Animals↗
PubMed1991

Number and topography of epitopes of human chorionic gonadotropin (hCG) are shared by desialylated and deglycosylated hCG.

A previously established map of the surface epitopes of human chorionic gonadotropin (hCG) served as template for the present study in which we investigated the antigenic surfaces of two glycosylation variants of hCG, i.e. desialylated hCG (asialo-hCG) and deglycosylated hCG (degly-hCG). This map allocates five epitopes to the alpha subunit, five to the beta subunit and four alpha beta epitopes to structures formed only by the alpha/beta heterodimer holo-hCG (Schwarz et al. (1986) Endocrinology 118, 189-197; Berger et al. (1990) J. Endocrinol. 125, 301-309). Here it is described that both variants complied with this template: each of the 14 distinct monoclonal antibodies with which the epitopes of hCG were defined reacted with radiolabeled asialo-hCG and degly-hCG as well and generally bound degly-hCG with greater affinity than hCG. Moreover, every combination of capture and radiolabeled detection antibody that was either compatible or incompatible on unlabeled hCG was so also on unlabeled asialo-hCG and degly-hCG. It thus appears that alterations of the carbohydrate structure of hCG can be associated with a change in affinity between some antibodies and their respective epitopes but not with a loss of an epitope or with a change in the topographical relationships of the 14 epitopes.

Antibodies, Monoclonal↗
PubMed1995

Identification of functional interaction sites on proteins using bacteriophage-displayed random epitope libraries.

We describe a phage-display-based method to identify epitopes or interaction sites on proteins. DNA encoding the protein of interest is partially degraded with DNase I to generate random fragments of 50-200 bp. These fragments are then cloned into a phagemid vector that has been modified to allow the expression of the random fragments and the construction of a (bacterio)phage-displayed random epitope library. Phages displaying functional epitopes can be selected from these libraries by affinity selection or panning. To test this method we have constructed a random-epitope library for human plasminogen-activator inhibitor 1 and used this library to map the epitope of a monoclonal antibody (mAb) directed against this protein. By alignment of the selected overlapping epitope-containing fragments, we were able to locate the epitope of the mAb on a stretch of 39 amino acids spanning from E128 to V166. The approach may also be applied to more complex systems than single-protein genes, such as viral genomes or complete cDNA libraries.

Amino Acid Sequence↗
PubMed1995

Developmental expression of tau proteins in the chicken and rat brain: rapid down-regulation of a paired helical filament epitope in the rat cerebral cortex coincides with the transition from immature to adult tau isoforms.

The monoclonal antibodies TAU-1 and AT8 are directed at human microtubule-associated protein tau epitopes that contain a dephosphorylated and phosphorylated Ser202, respectively, while AT180 and AT270 are anti-tau monoclonals with epitopes that require phosphorylated Thr181 and Thr231, respectively. We used these antibodies to study the developmental profiles of tau proteins in rat cerebral cortex and chicken optic lobes. In tau extracts from perinatal rat cerebral cortex. AT8 recognized one major protein band of approximately 50 kDa that peaks on postnatal day 6 and declines rapidly to lower levels at day 12. At later stages, the AT8 epitope was expressed by several adult tau isoforms that were, however, stained only very faintly in highly enriched samples. Two additional tau epitopes recognized by AT180 and AT270 were found to be expressed by one or two protein bands up to about postnatal day 19 and then declined. Unlike the AT8 epitope, in the mature brain these epitopes were stained strongly in enriched samples, where they were expressed by a greater number of adult isoforms. Between embryonic day 19 and postnatal day 12, TAU-1 was found to recognize one major protein band of approximately 50 kDa which migrated slightly faster than the AT8-binding band. At postnatal day 19 and all older stages (including adult cortex), at least three additional TAU-1-binding isoforms with higher apparent molecular weights were present. Hence, the transition from one immature to several adult TAU-1-binding tau isoforms between postnatal day 12 and 19 in rat cerebral cortex coincides with the phase of rapid down-regulation of the AT8 epitope. As in the rat cerebrum, in chicken optic lobes there is a developmental decrease of AT8-binding proteins which is paralleled by striking changes in the electrophoretic pattern of tau isoforms recognized by TAU-1. In both rat cerebral cortex and chicken optic lobes, the period of maximal expression of AT8-binding tau is morphologically characterized by intense axonal growth and beginning synaptogenesis, whereas its subsequent rapid down-regulation and the appearance of novel TAU-1-binding isoforms correlates with synaptic maturation, the onset of spontaneous electrical activity and the beginning of myelination.

Animals↗
PubMed1993

Fine specificity of antibody recognition of carcinoma-associated epithelial mucins: antibody binding to synthetic peptide epitopes.

The protein core of polymorphic epithelial mucins consists predominantly of a repeating 20 amino acid peptide motif. Many monoclonal antibodies reactive with breast carcinomas recognise determinants located within the mucin protein core, and epitope mapping techniques have demonstrated that these antibodies bind to epitopes of three, four or five amino acids within the hydrophilic sequence, P D T R P A P. Each of these mucin core-reactive antibodies map to epitopes containing the central arginine residue. The fine specificity of a panel of anti-mucin antibodies binding to the tetrameric peptides P D T R or R P A P (synthesised on the heads of polyethylene pins) was examined by systematically replacing each amino acid in turn with all other 19 natural amino acids, and then testing these analogues for antibody binding. We have (i) identified those amino acids in epitopes which are essential for antibody binding, (ii) shown that for each epitope there is a hierarchy of residues required for immune recognition--certain amino acids may be replaced with little or no loss of antibody binding, while the presence of others is essential, and (iii) concluded that antibody specificity is further regulated by the residue(s) flanking an epitope motif which may impose conformational constraints upon the presentation of the epitope to an antibody.

Amino Acid Sequence↗
PubMed2004

T cell epitope spreading to myelin oligodendrocyte glycoprotein in HLA-DR4 transgenic mice during experimental autoimmune encephalomyelitis.

Epitope spreading has been implicated in the pathogenesis of experimental autoimmune encephalomyelitis (EAE) and human multiple sclerosis (MS). T cell epitope spreading has been demonstrated in rodents for myelin basic protein (MBP) and proteolipid protein (PLP) determinants, but not for myelin oligodendrocyte glycoprotein (MOG), another important myelin antigen. Moreover, the role of human autoimmunity-associated MHC molecules in epitope spreading, including HLA-DR2 and DR4, has not been formally examined. To address these questions, we investigated epitope spreading to MOG determinants in HLA-DR4 (DRB1*0401) transgenic mice during EAE. The data show that upon induction of EAE in HLA-DR4 transgenic mice with the immunodominant HLA-DR4-restricted MOG peptide 97-108 (MOG(97-108); TCFFRDHSYQEE), the T cell response diversifies over time to MOG(181-200) (core: MOG(183-191); FVIVPVLGP) and MBP. The spreading epitope MOG(181-200) binds with high affinity to HLA-DRB1*0401 and is presented by human HLA-DRB1*0401+antigen presenting cells. Moreover, this epitope is encephalitogenic in HLA-DRB1*0401 transgenic mice. This study demonstrates intra- and intermolecular epitope spreading to MOG and MBP in "humanized" HLA-DR4 transgenic mice.

Animals↗
PubMed2005

Efficient promotion of collagen antibody induced arthritis (CAIA) using four monoclonal antibodies specific for the major epitopes recognized in both collagen induced arthritis and rheumatoid arthritis.

An antibody response to defined epitopes located on the triple helical portion of type II collagen (CII) is associated with the development of collagen-induced arthritis (CIA) and rheumatoid arthritis (RA). Monoclonal antibodies to epitopes associated with arthritis, but not antibodies specific for epitopes not associated with arthritis, induce arthritis in mice, the so-called collagen antibody induced arthritis (CAIA) model. We have selected monoclonal IgG antibodies specific for four well-defined major epitopes on triple helical CII, the C1, J1, D3 and U1 epitopes. These antibodies bind the epitopes specifically as determined using recombinant or synthetic triple helical epitopes. They are encoded from somatically mutated V genes. They all bind cartilage in vivo in normal mice. All of the antibodies induce mild arthritis after injection intravenously and if injected as a cocktail they induce severe clinical arthritis. Intravenous injection of a total of 4 mg antibodies (0.5 mg antibodies per clone) induced arthritis in several different mouse strains without any secondary immune stimulus and intraperitoneal injection of LPS 7 days later dramatically raised the severity. Thus, this method is recommended as a new protocol for the induction of CAIA.

Animals↗
PubMed2006

Fine and domain-level epitope mapping of botulinum neurotoxin type A neutralizing antibodies by yeast surface display.

Botulinum neurotoxin (BoNT), the most poisonous substance known, causes naturally occurring human disease (botulism) and is one of the top six biothreat agents. Botulism is treated with polyclonal antibodies produced in horses that are associated with a high incidence of systemic reactions. Human monoclonal antibodies (mAbs) are under development as a safer therapy. Identifying neutralizing epitopes on BoNTs is an important step in generating neutralizing mAbs, and has implications for vaccine development. Here, we show that the three domains of BoNT serotype A (BoNT/A) can be displayed on the surface of yeast and used to epitope map six mAbs to the toxin domains they bind. The use of yeast obviates the need to express and purify each domain, and it should prove possible to display domains of other BoNT subtypes and serotypes for epitope mapping. Using a library of yeast-displayed BoNT/A binding domain (H(C)) mutants and selecting for loss of binding, the fine epitopes of three neutralizing BoNT/A mAbs were identified. Two mAbs bind the C-terminal subdomain of H(C), with one binding near the toxin sialoganglioside binding site. The most potently neutralizing mAb binds the N-terminal subdomain of H(C), in an area not previously thought to be functionally important. Modeling the epitopes shows how all three mAbs could bind BoNT/A simultaneously and may explain, in part, the dramatic synergy observed on in vivo toxin neutralization when these antibodies are combined. The results demonstrate how yeast display can be used for domain-level and fine mapping of conformational BoNT antibody epitopes and the mapping results identify three neutralizing BoNT/A epitopes.

Antibodies, Bacterial↗
PubMed2006

Structural basis of enhanced binding of extended and helically constrained peptide epitopes of the broadly neutralizing HIV-1 antibody 4E10.

Potent, broadly HIV-1 neutralizing antibodies (nAbs) may be invaluable for the design of an AIDS vaccine. 4E10 is the broadest HIV-1 nAb known to date and recognizes a contiguous and highly conserved helical epitope in the membrane-proximal region of gp41. The 4E10 epitope is thus an excellent target for vaccine design as it is also highly amenable to peptide engineering to enhance its helical character. To investigate the structural effect of both increasing the peptide length and of introducing helix-promoting constraints in the 4E10 epitope, we have determined crystal structures of Fab 4E10 bound to an optimized peptide epitope (NWFDITNWLWYIKKKK-NH(2)), an Aib-constrained peptide epitope (NWFDITNAibLWRR-NH(2)), and a thioether-linked peptide (NWFCITOWLWKKKK-NH(2)) to resolutions of 1.7 A, 2.1 A, and 2.2 A, respectively. The thioether-linked peptide is the first reported structure of a cyclic tethered helical peptide bound to an antibody. The introduced helix constraints limit the conformational flexibility of the peptides without affecting interactions with 4E10. The substantial increase in affinity (10 nM versus 10(4) nM of the IC(50) of the original KGND peptide template) is largely realized by 4E10 interaction with an additional helical turn at the peptide C terminus that includes Leu679 and Trp680. Thus, the core 4E10 epitope was extended and modified to a WFX(I/L)(T/S)XX(L/I)W motif, where X does not play a major role in 4E10 binding and can be used to introduce helical-promoting constraints in the peptide epitope.

Amino Acid Sequence↗
PubMed2006

Vaccination with a HER2/neu peptide induces intra- and inter-antigenic epitope spreading in patients with early stage breast cancer.

BACKGROUND: We are conducting clinical vaccine trials with the HER2/neu peptide, E75, in patients with breast cancer. The purpose of this study was to demonstrate clonal expansion of E75-specific CD8(+) T cells and to identify intra- and interantigenic epitope spreading. METHOD: Pre- and postvaccination peripheral blood leukocyte samples (24 node positive [NP] and 20 node negative [NN]) from 44 vaccinated patients were analyzed. HLA-A2:Ig dimer molecules were loaded with the HER2 peptides, E75 or GP2, and were used with anti-TcR and CD8 antibodies to stain peripheral blood leukocyte immediately ex vivo and were analyzed with flow cytometry. In 8 randomly selected patients, dimers were loaded with the folate binding protein peptide E41 to evaluate for interantigenic epitope spreading. RESULTS: All patients with NP and 95% of the patients with NN showed E75-specific clonal expansion. Patients with NN showed more robust expansion. All patients with NP and 85% of the patients with NN showed evidence of intra-antigenic epitope that was spreading to GP2. However, patients with NN showed only moderate expansion to this subdominant epitope, which was not included in the immunizing mix. The degree of HER2/neu expression and disease stage impacted the ability to expand clonally E75- and GP2-specific CD8(+) T cells. Evidence of interantigenic epitope spreading to E41 was shown in 63% of the patients who were tested. CONCLUSION: Our data provide evidence for the induction of intra- and interantigenic epitope spreading that results from a single HER2/neu peptide vaccine even in early staged patients. The ability to raise immunity to multiple tumor antigens depends on both the degree of HER2/neu expression and the extent of disease. Epitope spreading is an essential element for the success of a peptide vaccine strategy.

Antigens, Neoplasm↗
PubMed2005

Identification of a novel immunodominant cytotoxic T lymphocyte epitope derived from human factor VIII in a murine model of hemophilia A.

Gene therapy of hemophilia A could be complicated by the development of immune responses against the vector as well as the Factor VIII (FVIII) transgene. Previous efforts have been focused on identifying FVIII inhibitor antibody epitopes, whereas the cytotoxic T lymphocyte (CTL) epitopes have not been characterized. CTL would kill cells expressing such epitopes and thus limit the efficacy of gene therapy. To investigate CTL responses against human FVIII in a mouse model of hemophilia A, a computer algorithm program (BIMAS) was employed to predict CTL epitopes of human FVIII. The potential binding of these predicted peptides to MHC class I K(b) was evaluated in a TAP-deficient cell line. When recombinant vaccinia virus expressing B domain-deleted human FVIII (vv-FVIII) was used to immunize E16 hemophilia A mice, a specific CTL response against FVIII152-159 was generated. In contrast, a CTL response to four other FVIII peptides was not detected. Therefore, FVIII152-159 represents a dominant CTL epitope. Identification of this epitope raises the possibility that CTL response to FVIII gene-transduced cells can be diminished by deliberatively mutating the dominant CTL epitope while retaining the biologic function of FVIII for hemophilia A gene therapy.

Algorithms↗
PubMed2006

Distribution of the alpha-gal epitope on adult porcine bone tissue.

INTRODUCTION: Bone xenografts from pig to human appear to be an alternative to resolve the shortage of bone autologous and allografts. However, the major obstacle of pig-to-human xenotransplantation is the interaction between human natural anti-Gal antibody and the alpha-Gal epitope abundantly expressed on pig endothelium. It was important to investigate the expression of alpha-Gal epitopes in porcine bone tissue to look for an ideal method to remove the alpha-Gal epitopes. METHODS: The cortical and trabecular bone were retrieved from five pigs. After the soft tissues and periosteum were removed, the blood and marrow cavity were cleaned with phosphate-buffered solution. All 5 mm x 5 mm x 5 mm samples were imbedded in paraffin and methyl methacrylate resin for histological sections. The mouse IgM M86 monoclonal antibody, which was highly specific for alpha-Gal epitopes, was used to document alpha-Gal epitope expression by immunostaining of tissues and immunofluorescence. RESULTS: Gal-positive immunostaining and immunofluorescence were observed on the surface of osteocytes and Haversian canals. There was a significant difference in Gal expression between cortical and trabecular bone tissues. There was no Gal expression in the extracellular matrix of bone. CONCLUSIONS: Major alpha-Gal epitopes were on the surface of osteocytes of porcine bone tissues. A method should be used to damage the osteocytes and eliminate the alpha-Gal epitopes to avoid the xenogenic rejection in xenotransplantation of porcine bone tissues.

Animals↗
PubMed2005

Antigen processing is predictable: From genes to T cell epitopes.

In order to induce a cellular immune response, antigens have to be processed in intracellular compartments, transported, and presented by HLA molecules prior to recognition by specific T cells. Many of the events that contribute to antigen processing have been thoroughly investigated during the past years and are now well understood, which lead to a number of prediction programs. "Reverse immunology" has been used for about 10 years in order to identify T cell epitopes from pathogens or tumor-associated antigens. The advantages and pitfalls of T cell epitope prediction compared to classical experimental procedures such as epitope mapping and cloning experiments have been discussed many times. In this presentation, a number of internet programs that offer help in T cell epitope prediction (or prediction of antigen processing) will be discussed in the light of transfusion medicine. Some databases are listing published HLA ligands and T cell epitopes, others offer epitope prediction for many HLA class I or class II restrictions. In addition, a number of established programs will be demonstrated which are freely accessible at no cost in the world wide web for the prediction of either HLA-peptide binding, proteasomal processing of antigens, or both. Epitope prediction and processing prediction programs will be applied to minor histocompatibility antigens (miHAgs) and compared. This reflects the actual possibilities and limitations of such computer-aided work not only in cellular immunology, but also in transplantation immunology.

Animals↗
PubMed2005

Identification of protective and non-protective T cell epitopes in influenza.

Understanding the immune response to different CD8 T cell epitopes is important for the development of vaccines designed to promote protective cellular immunity. Recently, we have shown that vaccination with the PA(224-233)/D(b) epitope of influenza virus was poorly protective in terms of viral clearance. To determine if other influenza virus epitopes behave in this manner, we analyzed the ability of three newly identified CD8 T cell epitopes and three previously defined epitopes to provide protection following vaccination and viral challenge. All six of the peptide-based vaccinations resulted in significantly increased numbers of epitope-specific CD8 T cells in the spleen. Interestingly, we found that vaccination with three peptides (HA(332-340), M1(128-135), or PA(224-233)) resulted in delayed viral clearance following infection. These findings indicate that some epitopes have a detrimental impact on viral clearance and have important implications for the development of vaccination strategies designed to provide protection against subsequent influenza virus challenge.

Animals↗
PubMed2006

Immunogenicity of a recombinant Mycobacterium bovis bacille Calmette-Guèrin expressing malarial and tuberculosis epitopes.

Recombinant Mycobacterium bovis bacille Calmette-Guèrin (rBCG) expressing the malarial epitopes F2R(II)EBA and (NANP)3 as well as two T cell epitopes of the M. tuberculosis ESAT-6 antigen, generated in favour of mycobacterium codon usage elicited specific immune response against these epitopes. Immunised Balb/c mice demonstrated an increase in almost all of the IgG subclasses against both malarial epitopes and enhanced splenocyte proliferative response against the malarial epitopes as well as selected peptides of ESAT-6. Furthermore, flow cytometric analyses showed elevated numbers of CD4+ lymphocytes expressing IFN-gamma and IL-2 against the ESAT-6 peptides, suggesting a specific Th1-mediated response. This study demonstrated that expressing malarial and TB epitopes in a single rBCG construct induced appropriate humoral and cellular immune response against immunogenic epitopes from both organisms.

Amino Acid Sequence↗
PubMed2006

Identification and characterization of novel neutralizing epitopes in the receptor-binding domain of SARS-CoV spike protein: revealing the critical antigenic determinants in inactivated SARS-CoV vaccine.

The spike (S) protein of severe acute respiratory syndrome coronavirus (SARS-CoV) is considered as a major antigen for vaccine design. We previously demonstrated that the receptor-binding domain (RBD: residues 318-510) of S protein contains multiple conformation-dependent neutralizing epitopes (Conf I to VI) and serves as a major target of SARS-CoV neutralization. Here, we further characterized the antigenic structure in the RBD by a panel of novel mAbs isolated from the mice immunized with an inactivated SARS-CoV vaccine. Ten of the RBD-specific mAbs were mapped to four distinct groups of conformational epitopes (designated Group A to D), and all of which had potent neutralizing activity against S protein-pseudotyped SARS viruses. Group A, B, C mAbs target the epitopes that may overlap with the previously characterized Conf I, III, and VI respectively, but they display different capacity to block the receptor binding. Group D mAb (S25) was directed against a unique epitope by its competitive binding. Two anti-RBD mAbs recognizing the linear epitopes (Group E) were mapped to the RBD residues 335-352 and 442-458, respectively, and none of them inhibited the receptor binding and virus entry. Surprisingly, most neutralizing epitopes (Groups A to C) could be completely disrupted by single amino acid substitutions (e.g., D429A, R441A or D454A) or by deletions of several amino acids at the N-terminal or C-terminal region of the RBD; however, the Group D epitope was not sensitive to the mutations, highlighting its importance for vaccine development. These data provide important information for understanding the antigenicity and immunogenicity of SARS-CoV, and this panel of novel mAbs can be used as tools for studying the structure of S protein and for guiding SARS vaccine design.

Animals↗
PubMed2006

Comparison of a fimbrial versus an autotransporter display system for viral epitopes on an attenuated Salmonella vaccine vector.

Attenuated Salmonella have been used as vectors to deliver foreign antigens as live vaccines. We have previously developed an efficient surface-display system by genetically engineering 987P fimbriae to present transmissible gastroenteritis virus (TGEV) C and A epitopes for the induction of anti-TGEV antibodies with a Salmonella vaccine vector. Here, this system was compared with an autotransporter protein surface display system. The TGEV C and A epitopes were fused to the passenger domain of the MisL autotransporter of Salmonella. Expression of both the MisL- and 987P subunit FasA-fusions to the TGEV epitopes were under the control of in vivo-induced promoters. Expression of the TGEV epitopes from the Salmonella typhimurium CS4552 (crp cya asd pgtE) vaccine strain was greater when the epitopes were fused to MisL than when they were fused to the 987P FasA subunit. However, when BALB/c mice were orally immunized with the Salmonella vector expressing the TGEV epitopes from either one of the fusion constructs or both together, the highest level of anti-TGEV antibody was obtained with the 987P-TGEV immunogen-displaying vector. This result suggested that better immune responses towards specific epitopes could be obtained by using a polymeric display system such as fimbriae.

Animals↗