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Fibronectin‐binding proteins secreted by Mycobacterium avium
Author(s) -
Kitaura HIDEKI,
Ohara NAOYA,
Naito MARIKO,
Kobayashi KAZUHIDE,
Yamada TAKESHI
Publication year - 2000
Publication title -
apmis
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.909
H-Index - 88
eISSN - 1600-0463
pISSN - 0903-4641
DOI - 10.1034/j.1600-0463.2000.d01-97.x
Subject(s) - fibronectin , microbiology and biotechnology , blot , extracellular , biology , gel electrophoresis , bacteria , extracellular matrix , antibody , chemistry , biochemistry , immunology , genetics , gene
Mycobacterium avium is an intracellular pathogen and a major opportunistic infectious agent observed in patients with acquired immune deficiency syndrome (AIDS). Fibronectin is an extracellular matrix protein and is a virulence factor for several extracellular pathogenic bacteria binding to mucosal surfaces. We investigated the fibronectin (FN)‐binding proteins in the culture filtrate of M. avium by two‐dimensional electrophoresis (2DE). Proteins in Sauton medium of M. avium after 3 weeks were separated by 2DE. The proteins were blotted onto polyvinylidene difluoride membrane and incubated with FN. FN‐binding proteins were detected by Western blotting using anti‐FN antibody. FN bound to five spots (33 kDa, 32 kDa, 31 kDa, 30 kDa and 25 kDa). N‐terminal amino acids of these were determined. The 33 kDa spot corresponded to antigen 85 (Ag 85) C. The 32 and 31 kDa spots were either Ag 85 A or Ag 85 B. The 30 kDa spot corresponded to Ag 85 B of M. avium. The 25 kDa spot corresponded to MPA51 (M. avium MPB51). Thus, FN bound exclusively to the Ag 85 complex and MPA51.