Identification and characterization of T helper cell epitopes of the major outer membrane protein of Chlamydia trachomatis.
Identifieur interne : 002865 ( PubMed/Checkpoint ); précédent : 002864; suivant : 002866Identification and characterization of T helper cell epitopes of the major outer membrane protein of Chlamydia trachomatis.
Auteurs : H. Su [États-Unis] ; R P Morrison ; N G Watkins ; H D CaldwellSource :
- The Journal of experimental medicine [ 0022-1007 ] ; 1990.
Descripteurs français
- KwdFr :
- Activation des lymphocytes (immunologie), Animaux, Anticorps antibactériens (biosynthèse), Anticorps antibactériens (immunologie), Chimère (immunologie), Chlamydia trachomatis (génétique), Chlamydia trachomatis (immunologie), Données de séquences moléculaires, Femelle, Immunisation, Lignées consanguines de souris, Lymphocytes B (immunologie), Lymphocytes T auxiliaires (immunologie), Peptides (administration et posologie), Peptides (immunologie), Peptides (synthèse chimique), Protéines de la membrane externe bactérienne (génétique), Protéines de la membrane externe bactérienne (immunologie), Protéines de la membrane externe bactérienne (synthèse chimique), Similitude de séquences d'acides nucléiques, Souris, Séquence d'acides aminés, Épitopes (immunologie).
- MESH :
- administration et posologie : Peptides.
- biosynthèse : Anticorps antibactériens.
- génétique : Chlamydia trachomatis, Protéines de la membrane externe bactérienne.
- immunologie : Activation des lymphocytes, Anticorps antibactériens, Chimère, Chlamydia trachomatis, Lymphocytes B, Lymphocytes T auxiliaires, Peptides, Protéines de la membrane externe bactérienne, Épitopes.
- synthèse chimique : Peptides, Protéines de la membrane externe bactérienne.
- Animaux, Données de séquences moléculaires, Femelle, Immunisation, Lignées consanguines de souris, Similitude de séquences d'acides nucléiques, Souris, Séquence d'acides aminés.
English descriptors
- KwdEn :
- Amino Acid Sequence, Animals, Antibodies, Bacterial (biosynthesis), Antibodies, Bacterial (immunology), B-Lymphocytes (immunology), Bacterial Outer Membrane Proteins (chemical synthesis), Bacterial Outer Membrane Proteins (genetics), Bacterial Outer Membrane Proteins (immunology), Chimera (immunology), Chlamydia trachomatis (genetics), Chlamydia trachomatis (immunology), Epitopes (immunology), Female, Immunization, Lymphocyte Activation (immunology), Mice, Mice, Inbred Strains, Molecular Sequence Data, Peptides (administration & dosage), Peptides (chemical synthesis), Peptides (immunology), Sequence Homology, Nucleic Acid, T-Lymphocytes, Helper-Inducer (immunology).
- MESH :
- chemical , administration & dosage : Peptides.
- chemical , biosynthesis : Antibodies, Bacterial.
- chemical , chemical synthesis : Bacterial Outer Membrane Proteins, Peptides.
- chemical , genetics : Bacterial Outer Membrane Proteins.
- chemical , immunology : Antibodies, Bacterial, Bacterial Outer Membrane Proteins, Epitopes, Peptides.
- genetics : Chlamydia trachomatis.
- immunology : B-Lymphocytes, Chimera, Chlamydia trachomatis, Lymphocyte Activation, T-Lymphocytes, Helper-Inducer.
- Amino Acid Sequence, Animals, Female, Immunization, Mice, Mice, Inbred Strains, Molecular Sequence Data, Sequence Homology, Nucleic Acid.
Abstract
Chlamydia trachomatis serovars A, B, and C are the causative agents of trachoma, the world's leading cause of preventable blindness. Immunoprophylaxis is a possible approach to control trachoma. The chlamydial major outer membrane protein (MOMP) is thought to play an important role in the development of protective immunity against chlamydial infection, and is therefore considered to be a promising candidate antigen in the development of a trachoma vaccine. Much effort has been focused on the molecular characterization of B cell sites of the MOMP that elicit neutralizing antibodies. Neutralizing sites have been identified as linear epitopes that reside within variable domains (VDs) of the protein whose primary sequences vary among different serovars. No information exists on MOMP T helper (Th) cell antigenic determinants, which are likely critical components for the development of a successful chlamydial vaccine. We used overlapping synthetic peptides (25 mers) representing the entire primary sequence of serovar A MOMP in T cell proliferation assays to identify T cell antigenic determinants of this molecule. Eight synthetic peptides (A-2, A-3, A-7, A-8, A-11, A-22, A-23, and A-24) stimulated proliferative responses of splenic T cells isolated from MOMP-immunized A/J mice. To ascertain if these peptides functioned as Th cell antigens, we determined their ability to prime A/J mice in vivo to produce an anamnestic IgG response specific to the MOMP. Mice primed with synthetic peptides A-8 (106-130) or A-23 (331-355) produced IgG antibodies reactive with the native MOMP and with the synthetic peptides corresponding to surface-accessible serovar-specific epitopes located in VD I and serogroup-specific epitopes located in VD IV of the protein. We synthesized the A-8 and A-23 peptides with the VD I sequence as colinear chimeric peptides. Immunization of mice with the T/B cell peptides produced high titered antibodies against the VD I sequence, and these antibodies reacted with the native MOMP and intact chlamydiae. The MOMP sequences containing these Th cell epitopes are conserved among the MOMP genes of different C. trachomatis serovars, indicating that they are common Th cell antigenic sites. Thus, the Th cell epitopes contained within these peptides, in combination with different trachoma serovar-specific B cell neutralizing determinants, may be useful in the development of a synthetic or recombinant trivalent trachoma vaccine.
DOI: 10.1084/jem.172.1.203
PubMed: 1694217
Affiliations:
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pubmed:1694217Le document en format XML
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<term>Bacterial Outer Membrane Proteins (chemical synthesis)</term>
<term>Bacterial Outer Membrane Proteins (genetics)</term>
<term>Bacterial Outer Membrane Proteins (immunology)</term>
<term>Chimera (immunology)</term>
<term>Chlamydia trachomatis (genetics)</term>
<term>Chlamydia trachomatis (immunology)</term>
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<term>Female</term>
<term>Immunization</term>
<term>Lymphocyte Activation (immunology)</term>
<term>Mice</term>
<term>Mice, Inbred Strains</term>
<term>Molecular Sequence Data</term>
<term>Peptides (administration & dosage)</term>
<term>Peptides (chemical synthesis)</term>
<term>Peptides (immunology)</term>
<term>Sequence Homology, Nucleic Acid</term>
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<term>Anticorps antibactériens (immunologie)</term>
<term>Chimère (immunologie)</term>
<term>Chlamydia trachomatis (génétique)</term>
<term>Chlamydia trachomatis (immunologie)</term>
<term>Données de séquences moléculaires</term>
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<term>Female</term>
<term>Immunization</term>
<term>Mice</term>
<term>Mice, Inbred Strains</term>
<term>Molecular Sequence Data</term>
<term>Sequence Homology, Nucleic Acid</term>
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<front><div type="abstract" xml:lang="en">Chlamydia trachomatis serovars A, B, and C are the causative agents of trachoma, the world's leading cause of preventable blindness. Immunoprophylaxis is a possible approach to control trachoma. The chlamydial major outer membrane protein (MOMP) is thought to play an important role in the development of protective immunity against chlamydial infection, and is therefore considered to be a promising candidate antigen in the development of a trachoma vaccine. Much effort has been focused on the molecular characterization of B cell sites of the MOMP that elicit neutralizing antibodies. Neutralizing sites have been identified as linear epitopes that reside within variable domains (VDs) of the protein whose primary sequences vary among different serovars. No information exists on MOMP T helper (Th) cell antigenic determinants, which are likely critical components for the development of a successful chlamydial vaccine. We used overlapping synthetic peptides (25 mers) representing the entire primary sequence of serovar A MOMP in T cell proliferation assays to identify T cell antigenic determinants of this molecule. Eight synthetic peptides (A-2, A-3, A-7, A-8, A-11, A-22, A-23, and A-24) stimulated proliferative responses of splenic T cells isolated from MOMP-immunized A/J mice. To ascertain if these peptides functioned as Th cell antigens, we determined their ability to prime A/J mice in vivo to produce an anamnestic IgG response specific to the MOMP. Mice primed with synthetic peptides A-8 (106-130) or A-23 (331-355) produced IgG antibodies reactive with the native MOMP and with the synthetic peptides corresponding to surface-accessible serovar-specific epitopes located in VD I and serogroup-specific epitopes located in VD IV of the protein. We synthesized the A-8 and A-23 peptides with the VD I sequence as colinear chimeric peptides. Immunization of mice with the T/B cell peptides produced high titered antibodies against the VD I sequence, and these antibodies reacted with the native MOMP and intact chlamydiae. The MOMP sequences containing these Th cell epitopes are conserved among the MOMP genes of different C. trachomatis serovars, indicating that they are common Th cell antigenic sites. Thus, the Th cell epitopes contained within these peptides, in combination with different trachoma serovar-specific B cell neutralizing determinants, may be useful in the development of a synthetic or recombinant trivalent trachoma vaccine.</div>
</front>
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<ArticleTitle>Identification and characterization of T helper cell epitopes of the major outer membrane protein of Chlamydia trachomatis.</ArticleTitle>
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<Abstract><AbstractText>Chlamydia trachomatis serovars A, B, and C are the causative agents of trachoma, the world's leading cause of preventable blindness. Immunoprophylaxis is a possible approach to control trachoma. The chlamydial major outer membrane protein (MOMP) is thought to play an important role in the development of protective immunity against chlamydial infection, and is therefore considered to be a promising candidate antigen in the development of a trachoma vaccine. Much effort has been focused on the molecular characterization of B cell sites of the MOMP that elicit neutralizing antibodies. Neutralizing sites have been identified as linear epitopes that reside within variable domains (VDs) of the protein whose primary sequences vary among different serovars. No information exists on MOMP T helper (Th) cell antigenic determinants, which are likely critical components for the development of a successful chlamydial vaccine. We used overlapping synthetic peptides (25 mers) representing the entire primary sequence of serovar A MOMP in T cell proliferation assays to identify T cell antigenic determinants of this molecule. Eight synthetic peptides (A-2, A-3, A-7, A-8, A-11, A-22, A-23, and A-24) stimulated proliferative responses of splenic T cells isolated from MOMP-immunized A/J mice. To ascertain if these peptides functioned as Th cell antigens, we determined their ability to prime A/J mice in vivo to produce an anamnestic IgG response specific to the MOMP. Mice primed with synthetic peptides A-8 (106-130) or A-23 (331-355) produced IgG antibodies reactive with the native MOMP and with the synthetic peptides corresponding to surface-accessible serovar-specific epitopes located in VD I and serogroup-specific epitopes located in VD IV of the protein. We synthesized the A-8 and A-23 peptides with the VD I sequence as colinear chimeric peptides. Immunization of mice with the T/B cell peptides produced high titered antibodies against the VD I sequence, and these antibodies reacted with the native MOMP and intact chlamydiae. The MOMP sequences containing these Th cell epitopes are conserved among the MOMP genes of different C. trachomatis serovars, indicating that they are common Th cell antigenic sites. Thus, the Th cell epitopes contained within these peptides, in combination with different trachoma serovar-specific B cell neutralizing determinants, may be useful in the development of a synthetic or recombinant trivalent trachoma vaccine.</AbstractText>
</Abstract>
<AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Su</LastName>
<ForeName>H</ForeName>
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