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Deduced amino acid sequences of class 1 protein (PorA) from three strains of Neisseria meningitidis. Synthetic peptides define the epitopes responsible for serosubtype specificity

Deduced amino acid sequences of class 1 protein (PorA) from three strains of Neisseria meningitidis. Synthetic peptides define the epitopes responsible for serosubtype specificity
Deduced amino acid sequences of class 1 protein (PorA) from three strains of Neisseria meningitidis. Synthetic peptides define the epitopes responsible for serosubtype specificity
The previously determined nucleotide sequence of the porA gene, encoding the class 1 outer membrane protein of meningococcal strain MC50, has been used to clone and sequence the porA gene from two further strains with differing serosubtype specificities. Comparison of the predicted amino acid sequences of the three class 1 proteins revealed considerable structural homology with major variation confined to two discrete regions (VR1 and VR2). The high degree of structural homology between the sequences gave predicted secondary structures that were almost identical, with the variable domains located in hydrophilic regions that are likely to be surface located and hence accessible to antibody binding. The predicted amino acid sequences have been used to define the epitopes recognized by mAbs with serosubtype specificity. A series of overlapping decapeptides spanning each of the class 1 protein sequences have been synthesized on solid-phase supports and probed with mAbs. Antibodies with P1.16 and P1.15 subtype specificity reacted with sequences in the VR2 domain, while antibodies with P1.7 subtype specificity reacted with sequences in the VR1 domain. Further peptides have been constructed to define the minimum epitopes recognized by each antibody. Thus we have been able to define linear peptides on each class 1 protein molecule that are responsible for subtype specificity and that represent targets for a protective immune response.
0022-1007
1871-1882
McGuinness, Brian
be5e0cb0-4361-4107-b4fa-c53eb310c82a
Barlow, Ann K.
95db0b89-4adb-487f-9fb3-dce009819c94
Clarke, Ian N.
ff6c9324-3547-4039-bb2c-10c0b3327a8b
Farley, John E.
58710321-f5e7-4dd5-87de-381f79e84880
Anilionis, Algis
76e019bb-7d19-43fd-9220-9c81b44e3502
Poolman, Jan T.
58502fd8-725f-441e-9916-7a098c0e9094
Heckels, John E.
fcfcfafe-5ca8-4728-9c5e-cb67f9af7e31
McGuinness, Brian
be5e0cb0-4361-4107-b4fa-c53eb310c82a
Barlow, Ann K.
95db0b89-4adb-487f-9fb3-dce009819c94
Clarke, Ian N.
ff6c9324-3547-4039-bb2c-10c0b3327a8b
Farley, John E.
58710321-f5e7-4dd5-87de-381f79e84880
Anilionis, Algis
76e019bb-7d19-43fd-9220-9c81b44e3502
Poolman, Jan T.
58502fd8-725f-441e-9916-7a098c0e9094
Heckels, John E.
fcfcfafe-5ca8-4728-9c5e-cb67f9af7e31

McGuinness, Brian, Barlow, Ann K., Clarke, Ian N., Farley, John E., Anilionis, Algis, Poolman, Jan T. and Heckels, John E. (1990) Deduced amino acid sequences of class 1 protein (PorA) from three strains of Neisseria meningitidis. Synthetic peptides define the epitopes responsible for serosubtype specificity. The Journal of Experimental Medicine, 171 (6), 1871-1882. (doi:10.1084/jem.171.6.1871). (PMID:1693651)

Record type: Article

Abstract

The previously determined nucleotide sequence of the porA gene, encoding the class 1 outer membrane protein of meningococcal strain MC50, has been used to clone and sequence the porA gene from two further strains with differing serosubtype specificities. Comparison of the predicted amino acid sequences of the three class 1 proteins revealed considerable structural homology with major variation confined to two discrete regions (VR1 and VR2). The high degree of structural homology between the sequences gave predicted secondary structures that were almost identical, with the variable domains located in hydrophilic regions that are likely to be surface located and hence accessible to antibody binding. The predicted amino acid sequences have been used to define the epitopes recognized by mAbs with serosubtype specificity. A series of overlapping decapeptides spanning each of the class 1 protein sequences have been synthesized on solid-phase supports and probed with mAbs. Antibodies with P1.16 and P1.15 subtype specificity reacted with sequences in the VR2 domain, while antibodies with P1.7 subtype specificity reacted with sequences in the VR1 domain. Further peptides have been constructed to define the minimum epitopes recognized by each antibody. Thus we have been able to define linear peptides on each class 1 protein molecule that are responsible for subtype specificity and that represent targets for a protective immune response.

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Published date: 1 June 1990
Organisations: Faculty of Medicine

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Local EPrints ID: 352634
URI: https://eprints.soton.ac.uk/id/eprint/352634
ISSN: 0022-1007
PURE UUID: 3dd95643-815b-4491-9943-b17bb6e7b57d
ORCID for Ian N. Clarke: ORCID iD orcid.org/0000-0002-4938-1620

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Date deposited: 04 Jun 2013 10:57
Last modified: 06 Jun 2018 13:19

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Author: Brian McGuinness
Author: Ann K. Barlow
Author: Ian N. Clarke ORCID iD
Author: John E. Farley
Author: Algis Anilionis
Author: Jan T. Poolman
Author: John E. Heckels

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