Epitope clusters in the major outer membrane protein of Chlamydia trachomatis
Identifieur interne : 001F37 ( Istex/Corpus ); précédent : 001F36; suivant : 001F38Epitope clusters in the major outer membrane protein of Chlamydia trachomatis
Auteurs : Seon-Kyeong Kim ; Robert DemarsSource :
- Current Opinion in Immunology [ 0952-7915 ] ; 2001.
English descriptors
- KwdEn :
- Teeft :
- Allotypes, Amino, Antibody responses, Antigenic, Cell epitope, Cell epitopes, Cell responses, Chlamydia, Chlamydia trachomatis, Chlamydial, Ctls, Cytosolic, Cytotoxic, Demars, Epitope, Epitope clusters, Genital, Genital tract infections, Immune, Immunization, Immunol, Immunology, Lymphocyte, Membrane protein, Momp, Mutant, Mutation, Original antigenic, Outer membrane protein, Pathogen, Peptide, Proteasomes, Protective immunity, Recurrent mutations, Serovar, Serovars, Trachomatis, Vaccine, Vaccine development.
Abstract
Abstract: Immunopathology that is caused by re-infection with Chlamydia trachomatis is very common in humans despite regular responses to multiple, often conserved, antibody and T cell epitopes. Recurrent mutations that disrupt T cell epitopes in the major outer membrane protein in clinical isolates and the reduced transcription of HLA genes by infected cells may be evidence for pathogen evasion of protective immune responses. Subunit vaccines containing recently discovered clusters of T cell epitopes in the major outer membrane protein that are presented with diverse HLA allotypes may allow widespread protective immunization while avoiding the suppression of lasting immunity that occurs by unknown mechanisms associated with infection.
Url:
DOI: 10.1016/S0952-7915(00)00237-5
Links to Exploration step
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<front><div type="abstract" xml:lang="en">Abstract: Immunopathology that is caused by re-infection with Chlamydia trachomatis is very common in humans despite regular responses to multiple, often conserved, antibody and T cell epitopes. Recurrent mutations that disrupt T cell epitopes in the major outer membrane protein in clinical isolates and the reduced transcription of HLA genes by infected cells may be evidence for pathogen evasion of protective immune responses. Subunit vaccines containing recently discovered clusters of T cell epitopes in the major outer membrane protein that are presented with diverse HLA allotypes may allow widespread protective immunization while avoiding the suppression of lasting immunity that occurs by unknown mechanisms associated with infection.</div>
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<note type="content">Fig. 1: CTL epitope map of MOMP. The mature MOMP protein is 370–374 amino acids long in different Ct strains and is anchored in the lipopolysaccharide (LPS)-containing outer membrane (OM) by five hydrophobic, membrane-spanning CSs (CS1–CS5 from amino terminus to carboxl terminus), which have amino acid sequences that are conserved in different strains. The CSs are linked by four surface-exposed VSs (shown as small, open squares) that vary greatly in amino acid sequence among strains of Ct and include neutralizing-antibody epitopes that define serovars. The positions on MOMP of nonamer CTL epitope sequences that are presented with HLA-A2, -B35, -B51 or -B62 ([26•,27]; Table 1) are labeled using arrows; the epitopes are classified using the residue numbers of their amino termini. (Schematic adapted from [11].)</note>
<note type="content">Fig. 2: MOMP CTL epitopes are located in HLA class I binding motif clusters. Nine-mer peptides from MOMP that have binding motifs for HLA-A1, -A2, -A3, -A11, -A24, -B7, -B8, -B27, -B35, -B44, -B51 or -B62 were identified with a National Institutes of Health (NIH) algorithm (http://bimas.dcrt.nih.gov/molbio/hla_bind/). Peptides that scored higher than 5 in predicted binding ability are shown as empty bars in their order along MOMP (the numbers above the MOMP CS/VS domain structure are amino acid positions). Black bars represent eight CTL epitopes that we identified in genital tract infections [26•,27] and two CTL epitopes (in CS1 and CS3) identified by others in ocular trachoma [30] (see Table 1). Hatched bars represent 16–22-mer peptides that induce proliferation of T helper cells from genitally infected individuals [28,29•]. The core epitopes in most of the Th-stimulatory peptides have not yet been defined; individual peptides shown may contain multiple core epitopes, as exemplified by the MOMP249–268 sequence shown in Fig. 3. Several Th-epitope-containing peptides identified by others [31,59] nearly coincide with those depicted and are not shown. VSs and CSs are as in [60].</note>
<note type="content">Fig. 3: CTL and Th epitopes are co-clustered in MOMP (see Fig. 1 for details of MOMP structure). The CTL epitope MOMP155, which spans VS2 and CS3, overlaps a Th-epitope-containing peptide (see Table 1) and is included within a sequence that was proposed to contain a human B cell epitope [50], the amino acid sequence of which has not been reported; (a) all of these epitopes are specifically associated with VS2 (boxed). (b) The amino acid sequence of MOMP249–268 is shown (in single-letter code); it has the largest number of human T cell epitopes reported for an antigenic 20-mer. The peptides that bind various common HLA allotypes are shown and include five known class I (HLA-B62, -B35 and -A2)-restricted minimal CTL epitopes [26•,27] and at least six known HLA class II (DR)-restricted minimal Th epitopes [28].</note>
<note type="content">Table 1: CTL epitopes overlap Th epitopes in C. trachomatis MOMP.</note>
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<ce:copyright type="full-transfer" year="2001">Elsevier Science Ltd</ce:copyright>
<ce:doctopics><ce:doctopic><ce:text>Immunity to infection</ce:text>
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<head><ce:dochead><ce:textfn>Review</ce:textfn>
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<ce:title>Epitope clusters in the major outer membrane protein of <ce:italic>Chlamydia trachomatis</ce:italic>
</ce:title>
<ce:author-group><ce:author><ce:given-name>Seon-Kyeong</ce:given-name>
<ce:surname>Kim</ce:surname>
<ce:cross-ref refid="AFF1"><ce:sup>a</ce:sup>
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<ce:e-address type="email">seonkim@stanford.edu</ce:e-address>
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<ce:author><ce:given-name>Robert</ce:given-name>
<ce:surname>DeMars</ce:surname>
<ce:cross-ref refid="AFF2"><ce:sup>b</ce:sup>
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<ce:e-address type="email">ridemars@facstaff.wisc.edu</ce:e-address>
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<ce:affiliation id="AFF1"><ce:label>a</ce:label>
<ce:textfn>Department of Microbiology and Immunology, Stanford University School of Medicine, 299 Campus Drive, Stanford, CA 94305, USA</ce:textfn>
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<ce:affiliation id="AFF2"><ce:label>b</ce:label>
<ce:textfn>Laboratory of Genetics, University of Wisconsin, 445 Henry Mall, Madison, WI 53706, USA</ce:textfn>
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<ce:abstract><ce:section-title>Abstract</ce:section-title>
<ce:abstract-sec><ce:simple-para>Immunopathology that is caused by re-infection with <ce:italic>Chlamydia trachomatis</ce:italic>
is very common in humans despite regular responses to multiple, often conserved, antibody and T cell epitopes. Recurrent mutations that disrupt T cell epitopes in the major outer membrane protein in clinical isolates and the reduced transcription of HLA genes by infected cells may be evidence for pathogen evasion of protective immune responses. Subunit vaccines containing recently discovered clusters of T cell epitopes in the major outer membrane protein that are presented with diverse HLA allotypes may allow widespread protective immunization while avoiding the suppression of lasting immunity that occurs by unknown mechanisms associated with infection.</ce:simple-para>
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<ce:keywords class="keyword"><ce:section-title>Keywords</ce:section-title>
<ce:keyword><ce:text>Chlamydia trachomatis</ce:text>
</ce:keyword>
<ce:keyword><ce:text>protective immunity</ce:text>
</ce:keyword>
<ce:keyword><ce:text>T cell epitopes</ce:text>
</ce:keyword>
<ce:keyword><ce:text>epitope cluster</ce:text>
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<ce:keyword><ce:text>MHC</ce:text>
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<ce:keyword><ce:text>vaccine</ce:text>
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<ce:keywords class="idt"><ce:section-title>Keywords</ce:section-title>
<ce:keyword><ce:text>Immunology</ce:text>
</ce:keyword>
<ce:keyword><ce:text>Microbiology</ce:text>
</ce:keyword>
<ce:keyword><ce:text>Drug Discovery</ce:text>
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<mods version="3.6"><titleInfo lang="en"><title>Epitope clusters in the major outer membrane protein of Chlamydia trachomatis</title>
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<name type="personal"><namePart type="given">Seon-Kyeong</namePart>
<namePart type="family">Kim</namePart>
<affiliation>E-mail: seonkim@stanford.edu</affiliation>
<affiliation>Department of Microbiology and Immunology, Stanford University School of Medicine, 299 Campus Drive, Stanford, CA 94305, USA</affiliation>
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<name type="personal"><namePart type="given">Robert</namePart>
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<abstract lang="en">Abstract: Immunopathology that is caused by re-infection with Chlamydia trachomatis is very common in humans despite regular responses to multiple, often conserved, antibody and T cell epitopes. Recurrent mutations that disrupt T cell epitopes in the major outer membrane protein in clinical isolates and the reduced transcription of HLA genes by infected cells may be evidence for pathogen evasion of protective immune responses. Subunit vaccines containing recently discovered clusters of T cell epitopes in the major outer membrane protein that are presented with diverse HLA allotypes may allow widespread protective immunization while avoiding the suppression of lasting immunity that occurs by unknown mechanisms associated with infection.</abstract>
<note type="content">Section title: Review</note>
<note type="content">Fig. 1: CTL epitope map of MOMP. The mature MOMP protein is 370–374 amino acids long in different Ct strains and is anchored in the lipopolysaccharide (LPS)-containing outer membrane (OM) by five hydrophobic, membrane-spanning CSs (CS1–CS5 from amino terminus to carboxl terminus), which have amino acid sequences that are conserved in different strains. The CSs are linked by four surface-exposed VSs (shown as small, open squares) that vary greatly in amino acid sequence among strains of Ct and include neutralizing-antibody epitopes that define serovars. The positions on MOMP of nonamer CTL epitope sequences that are presented with HLA-A2, -B35, -B51 or -B62 ([26•,27]; Table 1) are labeled using arrows; the epitopes are classified using the residue numbers of their amino termini. (Schematic adapted from [11].)</note>
<note type="content">Fig. 2: MOMP CTL epitopes are located in HLA class I binding motif clusters. Nine-mer peptides from MOMP that have binding motifs for HLA-A1, -A2, -A3, -A11, -A24, -B7, -B8, -B27, -B35, -B44, -B51 or -B62 were identified with a National Institutes of Health (NIH) algorithm (http://bimas.dcrt.nih.gov/molbio/hla_bind/). Peptides that scored higher than 5 in predicted binding ability are shown as empty bars in their order along MOMP (the numbers above the MOMP CS/VS domain structure are amino acid positions). Black bars represent eight CTL epitopes that we identified in genital tract infections [26•,27] and two CTL epitopes (in CS1 and CS3) identified by others in ocular trachoma [30] (see Table 1). Hatched bars represent 16–22-mer peptides that induce proliferation of T helper cells from genitally infected individuals [28,29•]. The core epitopes in most of the Th-stimulatory peptides have not yet been defined; individual peptides shown may contain multiple core epitopes, as exemplified by the MOMP249–268 sequence shown in Fig. 3. Several Th-epitope-containing peptides identified by others [31,59] nearly coincide with those depicted and are not shown. VSs and CSs are as in [60].</note>
<note type="content">Fig. 3: CTL and Th epitopes are co-clustered in MOMP (see Fig. 1 for details of MOMP structure). The CTL epitope MOMP155, which spans VS2 and CS3, overlaps a Th-epitope-containing peptide (see Table 1) and is included within a sequence that was proposed to contain a human B cell epitope [50], the amino acid sequence of which has not been reported; (a) all of these epitopes are specifically associated with VS2 (boxed). (b) The amino acid sequence of MOMP249–268 is shown (in single-letter code); it has the largest number of human T cell epitopes reported for an antigenic 20-mer. The peptides that bind various common HLA allotypes are shown and include five known class I (HLA-B62, -B35 and -A2)-restricted minimal CTL epitopes [26•,27] and at least six known HLA class II (DR)-restricted minimal Th epitopes [28].</note>
<note type="content">Table 1: CTL epitopes overlap Th epitopes in C. trachomatis MOMP.</note>
<subject><genre>article-category</genre>
<topic>Immunity to infection</topic>
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<subject lang="en"><genre>Keywords</genre>
<topic>Chlamydia trachomatis</topic>
<topic>protective immunity</topic>
<topic>T cell epitopes</topic>
<topic>epitope cluster</topic>
<topic>MHC</topic>
<topic>vaccine</topic>
</subject>
<subject lang="en"><genre>Keywords</genre>
<topic>Immunology</topic>
<topic>Microbiology</topic>
<topic>Drug Discovery</topic>
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