The adhesion of microbial pathogens to their target host cells is a highly specific process and a prerequisite for infection. To perform this function, pathogens have evolved molecules that display an intimate surface complementarity to extracellular host cell proteins, either in the external membrane or the extracellular matrix. In many cases, these microbial adhesins are able to replace native interactions in the host and trigger signalling cascades that 'cement' their binding and/or promote their internalisation into particular cell types. Importantly, these proteins are also among the first to interact with the immune system. As such, they represent good candidates for immunisation therapies and targets for drug design. Our research is focused in determining the structures of these molecules, their complexes with host cell receptors and to investigate the events that occur during the establishment of the infection.
et al., 2016, Candidalysin is a fungal peptide toxin critical for mucosal infection, Nature, Vol:532, ISSN:0028-0836, Pages:64-68
Cota E, Hoyer LL, 2015, The Candida albicans agglutinin-like sequence family of adhesins: functional insights gained from structural analysis, Future Microbiology, Vol:10, ISSN:1746-0921, Pages:1635-1648
et al., 2014, A proposed mechanism for the interaction between the Candida albicans Als3 adhesin and streptococcal cell wall proteins, Frontiers in Microbiology, Vol:5, ISSN:1664-302X
et al., 2014, The peptide-binding cavity Is essential for Als3-mediated adhesion of Candida albicans to human cells, Journal of Biological Chemistry, Vol:289, ISSN:1083-351X, Pages:18401-18412
et al., 2011, Structural basis for the broad specificity to host-cell ligands by the pathogenic fungus Candida albicans, Proceedings of the National Academy of Sciences of the United States of America, Vol:108, ISSN:0027-8424, Pages:15775-15779