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The Neisseria meningitidis macrophage infectivity potentiator (MIP) protein induces cross-strain serum bactericidal activity and is a potential serogroup B vaccine candidate

The Neisseria meningitidis macrophage infectivity potentiator (MIP) protein induces cross-strain serum bactericidal activity and is a potential serogroup B vaccine candidate
The Neisseria meningitidis macrophage infectivity potentiator (MIP) protein induces cross-strain serum bactericidal activity and is a potential serogroup B vaccine candidate
A gene encoding a 29kDa protein from Neisseria meningitidis serogroup B strain MC58, with homology to the macrophage infectivity potentiator (MIP) protein of Legionella pneumophila was cloned and expressed in Escherichia coli and the purified soluble recombinant protein (rMIP) was used for immunisation studies. Analysis of the predicted amino acid sequences of MIP from 13 well-characterised meningococcal strains, isolated from carriers or patients, and differing in serogroup, serotype and subtype, showed that the protein was highly conserved (98-100%) with only three distinct sequence types found (designated I, II and III). Western blotting showed that the MIP protein was expressed at similar levels by all of these strains. Immunisation of mice with type I MC58 rMIP in detergent micelles and liposomes containing monophosphoryl lipid A (MPLA) induced high levels of surface-reactive antibodies with serum bactericidal activity (SBA) titres of 1/1024 against the homologous strain. Bactericidal antibodies were also induced with the protein in saline alone and liposomes alone (titres of 1/128), but not following adsorption to Al(OH)3. Significantly, antisera raised against type I rMIP administered in saline or liposomes killed strains of heterologous sequence types II and III, with similar SBA titres (1/128-256). Taken together, these findings suggest that rMIP can provide cross-strain protection against meningococci and should be considered as a potential antigen for inclusion in new vaccines against meningococcal infection.
0019-9567
3784-3791
Hung, Miao-Chiu
bbf6cdc6-4a7a-403c-8d18-93e1dc9c3702
Salim, Omar
a8a00604-9e57-4638-8c96-5b37e75fee90
Williams, Jeanette N.
b8cee39f-8709-40ac-84ad-e62e3c1c7d8e
Heckels, John E.
fcfcfafe-5ca8-4728-9c5e-cb67f9af7e31
Christodoulides, Myron
eba99148-620c-452a-a334-c1a52ba94078
Hung, Miao-Chiu
bbf6cdc6-4a7a-403c-8d18-93e1dc9c3702
Salim, Omar
a8a00604-9e57-4638-8c96-5b37e75fee90
Williams, Jeanette N.
b8cee39f-8709-40ac-84ad-e62e3c1c7d8e
Heckels, John E.
fcfcfafe-5ca8-4728-9c5e-cb67f9af7e31
Christodoulides, Myron
eba99148-620c-452a-a334-c1a52ba94078

Hung, Miao-Chiu, Salim, Omar, Williams, Jeanette N., Heckels, John E. and Christodoulides, Myron (2011) The Neisseria meningitidis macrophage infectivity potentiator (MIP) protein induces cross-strain serum bactericidal activity and is a potential serogroup B vaccine candidate. Infection and Immunity, 79 (9), 3784-3791. (doi:10.1128/IAI.05019-11). (PMID:21708989)

Record type: Article

Abstract

A gene encoding a 29kDa protein from Neisseria meningitidis serogroup B strain MC58, with homology to the macrophage infectivity potentiator (MIP) protein of Legionella pneumophila was cloned and expressed in Escherichia coli and the purified soluble recombinant protein (rMIP) was used for immunisation studies. Analysis of the predicted amino acid sequences of MIP from 13 well-characterised meningococcal strains, isolated from carriers or patients, and differing in serogroup, serotype and subtype, showed that the protein was highly conserved (98-100%) with only three distinct sequence types found (designated I, II and III). Western blotting showed that the MIP protein was expressed at similar levels by all of these strains. Immunisation of mice with type I MC58 rMIP in detergent micelles and liposomes containing monophosphoryl lipid A (MPLA) induced high levels of surface-reactive antibodies with serum bactericidal activity (SBA) titres of 1/1024 against the homologous strain. Bactericidal antibodies were also induced with the protein in saline alone and liposomes alone (titres of 1/128), but not following adsorption to Al(OH)3. Significantly, antisera raised against type I rMIP administered in saline or liposomes killed strains of heterologous sequence types II and III, with similar SBA titres (1/128-256). Taken together, these findings suggest that rMIP can provide cross-strain protection against meningococci and should be considered as a potential antigen for inclusion in new vaccines against meningococcal infection.

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More information

Accepted/In Press date: 17 June 2011
e-pub ahead of print date: 27 June 2011
Published date: September 2011
Organisations: Infection Inflammation & Immunity

Identifiers

Local EPrints ID: 192017
URI: https://eprints.soton.ac.uk/id/eprint/192017
ISSN: 0019-9567
PURE UUID: 92335d46-ee7c-40af-b8cd-e662bc2ea7aa
ORCID for Omar Salim: ORCID iD orcid.org/0000-0002-2562-4827

Catalogue record

Date deposited: 29 Jun 2011 08:04
Last modified: 07 Aug 2019 00:46

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