Anaplasma phagocytophilum major surface protein-2 (Msp2) forms multimeric complexes in the bacterial membrane

Anaplasma phagocytophilum 44-kDa major surface protein-2 (Msp2) mediates partial neutrophil adhesion and interactions. Since A. phagocytophilum 44-kDa monoclonal antibodies also react with 160- and 100-kDa bands, a putative adhesin complex was studied. After separate excision/immunoprecipitation of...

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Bibliographic Details
Published in:FEMS microbiology letters 2003-10, Vol.227 (2), p.243-247
Main Authors: Park, Jinho, Kim, Kee Jun, Grab, Dennis J, Dumler, J Stephen
Format: Article
Language:English
Subjects:
Adhesion
Anaplasma phagocytophilum
Crosslinking
Electrophoresis
Gel electrophoresis
Immunoprecipitation
Microbiology
Monoclonal antibodies
Monomers
Neutrophils
Oligomerization
Polyacrylamide
Polymerization
Proteins
Sodium dodecyl sulfate
Sodium lauryl sulfate
Urea
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Summary:Anaplasma phagocytophilum 44-kDa major surface protein-2 (Msp2) mediates partial neutrophil adhesion and interactions. Since A. phagocytophilum 44-kDa monoclonal antibodies also react with 160- and 100-kDa bands, a putative adhesin complex was studied. After separate excision/immunoprecipitation of these three bands, sodium dodecyl sulfate–polyacrylamide gel electrophoresis (SDS–PAGE) resolved each into three bands again with increased 44-kDa protein under reducing conditions suggesting oligomerization of Msp2 44-kDa monomers. With 9 M urea, each separately excised band was resolved only into 44-kDa monomers with three different pIs. With protein cross-linking, immunoblots showed four additional bands and increased high molecular mass band intensity, suggesting homo- and hetero-polymerization with other A. phagocytophilum proteins. Recognition of Msp2 complexes facilitates understanding of A. phagocytophilum-neutrophil adhesion.
ISSN:0378-1097
1574-6968
DOI:10.1016/S0378-10970300687-6