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

摘要

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 p/s. 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. (C) 2003 Federation of European Microbiological Societies. Published by Elsevier B.V. All rights reserved. [References: 19]