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To study the role of a conidial cell wall-associated glycoprotein (Gp78) in the interaction of the entomopathogenic fungus Metarhizium robertsii with insect cuticles, gene deletion mutants were created by homologous recombination. The Gp78 locus was silenced by double-stranded RNA interference, and selected mutants were shown to be deficient in the synthesis of the protein. Analysis of the mutant conidia revealed that the glycosylation of Gp78 changed significantly in the mutant compared to the wild-type conidia, and that it was responsible for the migration of the protein to the growing tip of the conidium, where it is thought to play a role in cell-wall expansion. The mutant conidia were also found to be almost completely non-adhesive to the insect cuticle, while the wild-type conidia were found to be adherent. These results suggest that conidial Gp78 is important for effective adhesion of the fungus to insect cuticles.Generation of a humanized anti-HMGB1 monoclonal antibody for the treatment of sepsis in clinical trials.
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