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J Biol Chem, Vol. 275, Issue 4, 2415-2422, January 28, 2000
From the Institut de Pharmacologie et de Biologie Structurale du
CNRS, 205 route de Narbonne, 31077 Toulouse Cedex, France
The human pulmonary surfactant protein A (hSP-A)
has been implicated in the early capture and phagocytosis of the
pathogenic Mycobacterium tuberculosis by alveolar
macrophages. In this report, we examined the interaction of alveolar
proteinosis patient hSP-A with Mycobacterium bovis BCG, the
vaccinating strain, as a model of pathogenic mycobacteria, and
Mycobacterium smegmatis, a nonpathogenic strain. We found
that hSP-A binds to the surface of M. bovis BCG, but also
to a slightly lesser extent, to M. smegmatis, indicating that hSP-A does not discriminate between virulent and nonpathogenic strains. Among the various glycoconjugates isolated from the
mycobacterial envelope, we found that the best ligands are the two
major lipoglycans: the mannosylated lipoarabinomannan (ManLAM) and the
lipomannan. In contrast, the mannose-capped arabinomannan, structurally
close to the ManLAM, as well as the LAMs from the non pathogenic
M. smegmatis are poorly recognized by hSP-A. These results
clearly show that the presence of both the terminal mannose residues
and the phophatidyl-myo-inositol anchor are necessary to
achieve the highest binding affinity. Selective removal of either the
terminal mannose or the acyl residues esterifying the glycerol moiety
of the ManLAM abrogates the interaction with hSP-A, further supporting the notion that the hSP-A recognition of the carbohydrate epitopes of
the lipoglycans is dependent of the presence of the fatty acids.
To whom correspondence should be addressed: IPBS CNRS, 205 route
de Narbonne, 31077 Toulouse cedex, France. Tel.: 33-5-61-17-55-58; Fax:
33-5-61-17-59-94; E-mail: riviere@ipbs.fr.
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