Solubilization, isolation, and immunochemical characterization of the major outer membrane protein from Rhodopseudomonas sphaeroides.

ABSTRACT We used a photoactivatable, lipophilic reagent, 3′-(trifluoromethyl)-3-(m-[125I]iodophenyl)diazirine, to label proteins in the outer membrane of elementary bodies ofChlamydia trachomatis LGV serovar L2 and mass spectrometry to identify the labeled proteins. The identified proteins were polymorphic outer membrane proteins E, G, and H, which were made late in the developmental cycle, the major outer membrane protein, and a mixture of 46-kDa proteins consisting of the open reading frame 623 protein and possibly a modified form of the major outer membrane protein.

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Characterization of a major outer membrane protein multigene family in Ehrlichia ruminantium

Gene ◽

10.1016/j.gene.2004.01.020 ◽

2004 ◽

Vol 330 ◽

pp. 159-168 ◽

Cited By ~ 33

Author(s):

Henriette van Heerden ◽

Nicola E. Collins ◽

Kelly A. Brayton ◽

Celia Rademeyer ◽

Basil A. Allsopp

Keyword(s):

Membrane Protein ◽

Outer Membrane ◽

Outer Membrane Protein ◽

Multigene Family ◽

Major Outer Membrane Protein ◽

Ehrlichia Ruminantium

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Design, expression and functional characterization of a synthetic gene encoding the Chlamydia trachomatis major outer membrane protein

Gene ◽

10.1016/s0378-1119(00)00367-x ◽

2000 ◽

Vol 258 (1-2) ◽

pp. 173-181 ◽

Cited By ~ 9

Author(s):

H.Martin Jones ◽

Aya Kubo ◽

Richard S. Stephens

Keyword(s):

Chlamydia Trachomatis ◽

Membrane Protein ◽

Outer Membrane ◽

Outer Membrane Protein ◽

Functional Characterization ◽

Major Outer Membrane Protein ◽

Synthetic Gene ◽

Gene Encoding

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Production of a Monoclonal Antibody Specific for the Major Outer Membrane Protein of Campylobacter jejuni and Characterization of the Epitope

Applied and Environmental Microbiology ◽

10.1128/aem.01559-07 ◽

2007 ◽

Vol 74 (3) ◽

pp. 833-839 ◽

Cited By ~ 7

Author(s):

Hongliang Qian ◽

Ervinna Pang ◽

Qingyun Du ◽

Jason Chang ◽

Jin Dong ◽

...

Keyword(s):

Membrane Protein ◽

Outer Membrane ◽

Campylobacter Jejuni ◽

Outer Membrane Protein ◽

Protein Band ◽

Major Outer Membrane Protein ◽

Dot Blot ◽

Detection And Identification ◽

Dot Blot Assay

ABSTRACT Campylobacter species are important enteric pathogens causing disease in humans and animals. There is a lack of a good immunological test that can be used routinely to separate Campylobacter jejuni from other Campylobacter species. We produced monoclonal antibodies (MAbs) directed against the major outer membrane protein (MOMP) of C. jejuni using recombinant MOMP as the antigen. One MAb, designated MAb5C4 and of the immunoglobulin G1 isotype, was found to be potentially specific for C. jejuni. Dot blots demonstrated that MAb5C4 reacted with all 29 isolates of C. jejuni tested but did not react with 2 C. jejuni isolates, 26 other Campylobacter spp. isolates, and 19 non-Campylobacter isolates. Western blotting showed that MAb5C4 bound to a single protein band approximately 43 kDa in size, corresponding to the expected size of C. jejuni MOMP. The detection limit of MAb5C4 in a dot blot assay was determined to be about 5 × 103 bacteria. The epitope on the MOMP was mapped to a region six amino acids in length with the sequence 216GGQFNP221, which is 97% conserved among C. jejuni strains but divergent in other Campylobacter spp.; a GenBank search indicated that 95% of C. jejuni isolates will be able to be detected from non-Campylobacter spp. based on the highly specific and conserved region of the GGQFNP polypeptide. The epitope is predicted to be located in a region that is exposed to the periplasm. MAb5C4 is a potentially specific and sensitive MAb that can be used for the specific detection and identification of C. jejuni.

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