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.
Park
Jinho
J
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.
Kim
Kee Jun
KJ
Grab
Dennis J
DJ
Dumler
J Stephen
JS
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