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,
* Department of Cell Biology, Neurobiology, and Anatomy and
Department of Internal Medicine, Division of Infectious Diseases, University of Cincinnati College of Medicine, and
Research Division, Veterans Administration Medical Center, Cincinnati, OH 45267
Histoplasma capsulatum (Hc), is a facultative
intracellular fungus that binds to CD11/CD18 receptors on macrophages
(M
). To identify the ligand(s) on Hc yeasts that is recognized by
M, purified human complement receptor type 3 (CR3, CD11b/CD18) was
used to probe a Far Western blot of a detergent extract of Hc cell wall
and cell membrane. CR3 recognized a single 60-kDa protein, which was
identified as heat shock protein 60 (hsp60). Biotinylation of viable
yeasts, followed by precipitation with streptavidin-coated beads, and
Western blotting with anti-hsp60 demonstrated that hsp60 was on the
surface of Hc yeasts. Electron and confocal microscopy revealed that
hsp60 resided on the yeast cell wall in discrete clusters. Recombinant
hsp60 (rhsp60) inhibited attachment of Hc yeasts to M. Recombinant
hsp60 and Abs to CD11b and CD18 inhibited binding of yeasts to Chinese
hamster ovary cells transfected with CR3 (CHO3). Polystyrene beads
coated with rhsp60 bound to M, and attachment was inhibited by Abs
to CD11 and CD18. Freeze/thaw extract (F/TE), a preparation of Hc yeast
surface proteins that contained hsp60, inhibited the attachment of Hc
yeasts to M. Depletion of hsp60 from F/TE removed the capacity of
F/TE to block binding of Hc to M. Interestingly, rhsp60 did not
inhibit binding of Hc yeasts to dendritic cells (DC), which recognize
Hc via very late Ag 5. Moreover, F/TE inhibited attachment of Hc to DC
even when depleted of hsp60. Thus, Hc hsp60 appears to be a major
ligand that mediates attachment of Hc to M CD11/CD18, whereas DC
recognize Hc via a different ligand(s).
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