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

Jinho Park, Kee Jun Kim, Dennis J. Grab, J. Stephen Dumler

Research output: Contribution to journalArticlepeer-review

Abstract

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.

Original languageEnglish (US)
Pages (from-to)243-247
Number of pages5
JournalFEMS microbiology letters
Volume227
Issue number2
DOIs
StatePublished - Oct 24 2003

Keywords

  • Adhesin
  • Anaplasma phagocytophilum
  • Ehrlichiosis
  • Major surface protein-2
  • Neutrophil
  • Rickettsia

ASJC Scopus subject areas

  • Microbiology
  • Molecular Biology
  • Genetics

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