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 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.
Division of Medical Microbiology, Department of Pathology, The Johns Hopkins University School of Medicine, Ross Research Building, Room 624, 720 Rutland Avenue, Baltimore, MD 21205, USA.
Jinho
J
Park
Kee Jun
KJ
Kim
Dennis J
DJ
Grab
J Stephen
JS
Dumler
D041081:Anaplasma phagocytophilum / Q000276:immunology / Q000378:metabolism*; D001422:Bacterial Adhesion / Q000502:physiology*; D001425:Bacterial Outer Membrane Proteins / Q000378:metabolism*; D018929:Cell Culture Techniques; D008562:Membrane Glycoproteins / Q000378:metabolism; D009504:Neutrophils / Q000382:microbiology
D001425:Bacterial Outer Membrane Proteins; D008562:Membrane Glycoproteins; C488283:msp2 protein, Anaplasma phagocytophilum; C450839:p44 protein, Anaplasma phagocytophila