One fraction of mannoprotein has been very less important in the mutant strain.

We have attempted to relate mannoprotein constituents to the microbial function and (or) host response.

Key words: adherence, complement receptor, mannoprotein, virulence, ligand recognition.

For instance, we have recently found that a protein moiety of a 65-kDa mannoprotein is a major target of cell-mediated immune response.

Hwp1 is a mannoprotein located on the surface of the hyphae in the hyphal form of Candida albicans.

Lectinlike interactions have been identified between the protein portion of two mannoprotein adhesins and glycosides containing L-fucose or N-acetylglucosamine.

Other mannoprotein adhesins proposed recently include the factor 6 epitope present on serotype A strains of C. albicans and an integrin analogue.

This adhesion involves adhesins (e.g., hyphal wall protein 1), and extracellular polymeric materials (e.g., mannoprotein).

Hyphal forms of the organism possess a 60-kDa mannoprotein that recognizes a variety of host-cell ligands including the complement C3 conversion products, C3bi and C3d.

Overall, these studies emphasize the need for further definition of individual mannoprotein constituents to dissect the multiple biological actions of these highly complex, multifunctional molecular within C. albicans.

The increased synthesis of 30- to 32-kDa acidic polypeptides, together with the decreased accumulation of a prominent 95-kDa mannoprotein provided evidence for major alterations of Pisolithus tinctorius cell walls during mycorrhiza formation.

Candida albicans is a human commensal and opportunistic fungal organism that expresses on its surface and releases into the external milieu a variety of mannoprotein molecules that are relevant in many aspects of host–Candida relationship.