ArticleInfection and immunity2000
Identification of murine B-cell and T-cell epitopes of Escherichia coli outer membrane protein F with synthetic polypeptides.
Article in Infection and immunity, 2000. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.
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Who cites it
15 citing papers in PubMed, 21 citations in OpenAlex.
- Outgrowth of Escherichia is susceptible to aggravation of systemic lupus erythematosus.Arthritis research & therapy · 2024Article
- Stable expression of HIV-1 MPER extended epitope on the surface of the recombinant probiotic bacteria Escherichia Coli Nissle 1917 using CRISPR/Cas9.Microbial cell factories · 2024Article
- Article
- Molecular Characterization, Phylogenetic, Expression, and Protective Immunity Analysis of OmpF, a Promising Candidate Immunogen AgainstFrontiers in immunology · 2018Article
- Escherichia coli outer membrane protein F (OmpF): an immunogenic protein induces cross-reactive antibodies against Escherichia coli and Shigella.AMB Express · 2017Article
- Epitope-specific immune recognition of the nontypeable Haemophilus influenzae outer membrane protein 26.Human vaccines & immunotherapeutics · 2013Article
- Article
- Mucosal immunization with the Moraxella Catarrhalis porin m35 induces enhanced bacterial clearance from the lung: a possible role for opsonophagocytosis.Frontiers in immunology · 2011Article
- An efficient visualization tool for the analysis of protein mutation matrices.BMC bioinformatics · 2008Article
- Genes under positive selection in Escherichia coli.Genome research · 2007Article
- Fasciola hepatica: identification of CD4+ T-helper epitopes from the 11.5 kDa saposin-like protein SAP-2 using synthetic peptides.Experimental parasitology · 2007Article
- Protection against P. aeruginosa with an adenovirus vector containing an OprF epitope in the capsid.The Journal of clinical investigation · 2005Article
- Identification of an I-Ed-restricted T-cell epitope of Escherichia coli outer membrane protein F.Infection and immunity · 2004Article
- Nonhuman primate model for Listeria monocytogenes-induced stillbirths.Infection and immunity · 2003Article
- Identification of canine helper T-cell epitopes from the fusion protein of canine distemper virus.Immunology · 2001Article
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The major pore-forming outer membrane proteins (Omps) of gram-negative bacteria demonstrate numerous immunomodulating properties and are involved in the virulence of pathogenic strains. Because Escherichia coli OmpF is the best-characterized porin in terms of structural and functional characteristics, in vitro B-cell and T-cell responses to this porin in six different strains of mice were analyzed. Mice were immunized with purified OmpF trimers or overlapping synthetic polypeptides (20-mers) spanning the entire 340-amino-acid sequence of the OmpF monomer. T-cell proliferative responses and immunoglobulin G antibody responses to native OmpF and the peptide analogues were determined. For each strain, patterns of T-cell proliferation were similar regardless of whether native OmpF or synthetic peptides were inoculated, although all strains recognized one or more cryptic determinants. Mice exhibited several haplotype-specific responses, but genetically permissive epitopes were also identified. Four peptides (75-94, 265-284, 295-314, and 305-324) elicited strong T-cell proliferative responses from all strains of mice when mice were presensitized with native OmpF or a homologous peptide. In general, 10 or fewer peptides were recognized by sera from mice immunized with native OmpF or synthetic peptides, and most sera from peptide-immunized mice reacted poorly with the native protein. Four peptides spanning amino acids 45 to 64, 95 to 114, 115 to 134, and 275 to 294 were recognized by sera from all strains immunized with native OmpF but not by sera from peptide-immunized mice. Peptides 245-264 and 305-324 were universally recognized by sera from peptide-immunized mice, but these sera reacted weakly or were negative when tested against the native protein. Based on the pattern of cytokine secretion by proliferating T cells, immunization with native OmpF polarizes T helper cells toward development of a TH1 response. T-cell and B-cell responses have been investigated based on the assumption that differences in epitope specificity could influence protective or pathologic host reactions. Because of the high level of structural homology of OmpF to porins isolated from other enteric pathogens, the identification of T- and B-cell-stimulatory determinants of E. coli OmpF may have broader application.
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