MersV1, Ncbi, Merge, bibRecord, 000243

Conformational epitopes recognized by protective anti-neisserial surface protein A antibodies.

Identifieur interne : 000243 ( Ncbi/Merge ); précédent : 000242; suivant : 000244

Conformational epitopes recognized by protective anti-neisserial surface protein A antibodies.

Auteurs : Victor C. Hou [États-Unis] ; Gregory R. Moe ; Zyde Raad ; Tomi Wuorimaa ; Dan M. Granoff

Source :

Infection and immunity [ 0019-9567 ] ; 2003.

RBID : pubmed:14638771

Descripteurs français

KwdFr :
- Animaux, Anticorps monoclonaux (immunologie), Conformation des protéines, Données de séquences moléculaires, Humains, Liposomes, Modèles moléculaires, Mutagenèse dirigée, Neisseria meningitidis (immunologie), Pliage des protéines, Protéines de la membrane externe bactérienne (), Protéines de la membrane externe bactérienne (génétique), Protéines de la membrane externe bactérienne (immunologie), Protéines recombinantes, Rats, Souris, Séquence d'acides aminés, Épitopes (immunologie).
MESH :

English descriptors

KwdEn :
- Amino Acid Sequence, Animals, Antibodies, Monoclonal (immunology), Bacterial Outer Membrane Proteins (chemistry), Bacterial Outer Membrane Proteins (genetics), Bacterial Outer Membrane Proteins (immunology), Epitopes (immunology), Humans, Liposomes, Mice, Models, Molecular, Molecular Sequence Data, Mutagenesis, Site-Directed, Neisseria meningitidis (immunology), Protein Conformation, Protein Folding, Rats, Recombinant Proteins.
MESH :
- chemical , chemistry : Bacterial Outer Membrane Proteins.
- chemical , genetics : Bacterial Outer Membrane Proteins.
- chemical , immunology : Antibodies, Monoclonal, Bacterial Outer Membrane Proteins, Epitopes.
- immunology : Neisseria meningitidis.
- Amino Acid Sequence, Animals, Humans, Liposomes, Mice, Models, Molecular, Molecular Sequence Data, Mutagenesis, Site-Directed, Protein Conformation, Protein Folding, Rats, Recombinant Proteins.

Abstract

NspA is a conserved membrane protein that elicits protective antibody responses in mice against Neisseria meningitidis. A recent crystallographic study showed that NspA adopts an eight-stranded beta-barrel structure when reconstituted in detergent. In order to define the segments of NspA-containing epitopes recognized by protective murine anti-NspA antibodies, we studied the binding of two bactericidal and protective anti-NspA monoclonal antibodies (MAbs), AL12 and 14C7. Neither MAb binds to overlapping synthetic peptides (10-mers, 12-mers, and cyclic 12-mers) corresponding to the entire mature sequence of NspA, or to denatured recombinant NspA (rNspA), although binding to the protein can be restored by refolding in liposomes. Based on the ability of the two MAbs to bind to Escherichia coli microvesicles prepared from a set of rNspA variants created by site-specific mutagenesis, the most important contacts between the MAbs and NspA appear to be located within the LGG segment of loop 3. The conformation of loop 2 also appears to be an important determinant, as particular combinations of residues in this segment resulted in loss of antibody binding. Thus, the two anti-NspA MAbs recognize discontinuous conformational epitopes that result from the close proximity of loops 2 and 3 in the three-dimensional structure of NspA. The data suggest that optimally immunogenic vaccines using rNspA will require formulations that permit proper folding of the protein.

DOI: 10.1128/iai.71.12.6844-6849.2003
PubMed: 14638771

Links toward previous steps (curation, corpus...)

to stream PubMed, to step Corpus: 002426
to stream PubMed, to step Curation: 002426
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Links to Exploration step

pubmed:14638771

Le document en format XML

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<front><div type="abstract" xml:lang="en">NspA is a conserved membrane protein that elicits protective antibody responses in mice against Neisseria meningitidis. A recent crystallographic study showed that NspA adopts an eight-stranded beta-barrel structure when reconstituted in detergent. In order to define the segments of NspA-containing epitopes recognized by protective murine anti-NspA antibodies, we studied the binding of two bactericidal and protective anti-NspA monoclonal antibodies (MAbs), AL12 and 14C7. Neither MAb binds to overlapping synthetic peptides (10-mers, 12-mers, and cyclic 12-mers) corresponding to the entire mature sequence of NspA, or to denatured recombinant NspA (rNspA), although binding to the protein can be restored by refolding in liposomes. Based on the ability of the two MAbs to bind to Escherichia coli microvesicles prepared from a set of rNspA variants created by site-specific mutagenesis, the most important contacts between the MAbs and NspA appear to be located within the LGG segment of loop 3. The conformation of loop 2 also appears to be an important determinant, as particular combinations of residues in this segment resulted in loss of antibody binding. Thus, the two anti-NspA MAbs recognize discontinuous conformational epitopes that result from the close proximity of loops 2 and 3 in the three-dimensional structure of NspA. The data suggest that optimally immunogenic vaccines using rNspA will require formulations that permit proper folding of the protein.</div>
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<Abstract><AbstractText>NspA is a conserved membrane protein that elicits protective antibody responses in mice against Neisseria meningitidis. A recent crystallographic study showed that NspA adopts an eight-stranded beta-barrel structure when reconstituted in detergent. In order to define the segments of NspA-containing epitopes recognized by protective murine anti-NspA antibodies, we studied the binding of two bactericidal and protective anti-NspA monoclonal antibodies (MAbs), AL12 and 14C7. Neither MAb binds to overlapping synthetic peptides (10-mers, 12-mers, and cyclic 12-mers) corresponding to the entire mature sequence of NspA, or to denatured recombinant NspA (rNspA), although binding to the protein can be restored by refolding in liposomes. Based on the ability of the two MAbs to bind to Escherichia coli microvesicles prepared from a set of rNspA variants created by site-specific mutagenesis, the most important contacts between the MAbs and NspA appear to be located within the LGG segment of loop 3. The conformation of loop 2 also appears to be an important determinant, as particular combinations of residues in this segment resulted in loss of antibody binding. Thus, the two anti-NspA MAbs recognize discontinuous conformational epitopes that result from the close proximity of loops 2 and 3 in the three-dimensional structure of NspA. The data suggest that optimally immunogenic vaccines using rNspA will require formulations that permit proper folding of the protein.</AbstractText>
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</noCountry>
<country name="États-Unis"><region name="Californie"><name sortKey="Hou, Victor C" sort="Hou, Victor C" uniqKey="Hou V" first="Victor C" last="Hou">Victor C. Hou</name>
</region>
</country>
</tree>
</affiliations>
</record>

Pour manipuler ce document sous Unix (Dilib)

EXPLOR_STEP=$WICRI_ROOT/Sante/explor/MersV1/Data/Ncbi/Merge

HfdSelect -h $EXPLOR_STEP/biblio.hfd -nk 000243 | SxmlIndent | more

HfdSelect -h $EXPLOR_AREA/Data/Ncbi/Merge/biblio.hfd -nk 000243 | SxmlIndent | more

Pour mettre un lien sur cette page dans le réseau Wicri

{{Explor lien
   |wiki=    Sante
   |area=    MersV1
   |flux=    Ncbi
   |étape=   Merge
   |type=    RBID
   |clé=     pubmed:14638771
   |texte=   Conformational epitopes recognized by protective anti-neisserial surface protein A antibodies.
}}

Pour générer des pages wiki

HfdIndexSelect -h $EXPLOR_AREA/Data/Ncbi/Merge/RBID.i   -Sk "pubmed:14638771" \
       | HfdSelect -Kh $EXPLOR_AREA/Data/Ncbi/Merge/biblio.hfd   \
       | NlmPubMed2Wicri -a MersV1

This area was generated with Dilib version V0.6.33.
Data generation: Mon Apr 20 23:26:43 2020. Site generation: Sat Mar 27 09:06:09 2021

	Serveur d'exploration MERS
	Attention, ce site est en cours de développement ! Attention, site généré par des moyens informatiques à partir de corpus bruts. Les informations ne sont donc pas validées.

Serveur d'exploration MERS

Conformational epitopes recognized by protective anti-neisserial surface protein A antibodies.

Conformational epitopes recognized by protective anti-neisserial surface protein A antibodies.

Source :

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Abstract

Links toward previous steps (curation, corpus...)

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Le document en format XML

Pour manipuler ce document sous Unix (Dilib)

Pour mettre un lien sur cette page dans le réseau Wicri

Pour générer des pages wiki