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J Biol Chem, Vol. 273, Issue 5, 2905-2909, January 30, 1998
The Novel Fibronectin-binding Motif and Key Residues of
Mycobacteria
Mariko
Naito,
Naoya
Ohara,
Sohkichi
Matsumoto, and
Takeshi
Yamada
From the Department of Oral Bacteriology, Nagasaki University
School of Dentistry, 1-7-1 Sakamoto, Nagasaki 852, Japan
The binding motifs of the immunodominant antigen
(Ag) -Ag (Ag 85 complex B) of Mycobacterium kansasii for
human fibronectin were examined using digested fragments. We defined
two fibronectin-binding epitopes on 27 amino acids from 84 to 110 and
on 20 amino acids from 211 to 230. The epitopes were almost conserved
in the closely related Ag 85 complex of other mycobacteria species.
Inhibition of fibronectin binding to intact -Ag molecules was
observed with peptide-(84-110), but not with peptide-(211-230).
Peptide-(84-110) could also inhibit fibronectin binding to all
components of the Ag 85 complex of Bacillus Calmette-Guérin (Ag
85A, Ag 85B, and Ag 85C). Further study with synthetic peptides defined
11 residues from 98 to 108 as the minimum motif. Six residues
(98FEWYYQ103) were critical for interacting
with fibronectin. The motif revealed no homology to other known
prokaryotic and eukaryotic fibronectin-binding proteins. The defined
motif of -Ag is novel and unique for mycobacteria.
Copyright © 1998 by The American Society for Biochemistry and Molecular Biology, Inc.

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Copyright © 1998 by the American Society for Biochemistry and Molecular Biology.
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