BBB Seminar: Juan A. Hermoso
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Unraveling the host-pathogen interactions in Streptococcus pneumoniae by X-ray crystallography
Department of Crystallography and Structural Biology, Institute of Physical Chemistry 鈥淩ocasolano鈥�, Spanish National Research Council (CSIC), Madrid, Spain
Streptococcus pneumoniae is a human pathogen responsible for some of the infection diseases with higher index of mortality and morbidity worldwide. S. pneumoniae displays on its surface numerous proteins, the majority of which are virulence factors that contribute to the pathogenesis of this organism. Such proteins participate in specific interactions with human host tissues, thereby facilitating bacterial survival, helping the organism spread within host tissues, and concealing the bacterial surface from the host鈥檚 defence mechanism. We are involved in the study of virulence mechanisms mediated by pneumococcal surface proteins, the host proteins involved in pathogen recognition and the structural characterization of novel endolysins (phage-encoded enzymes that break down bacterial peptidoglycan) with potential application as antibacterial agents (enzybiotics). Recent research has not only revealed the surprising rich structural catalytic diversity of these surface proteins but has also yielded insights into their modular organization, their mechanism of recognition of the bacterial cell wall, and their implications in pneumococcal pathogenesis. Perspectives and future research will be also discussed.
Selected references:
Hermoso et al., Nature Structural & Molecular Biology (2005) 12:533-8
Hermoso et al., Current Opinion in Microbiology (2007). 10:461-72
笔茅谤别锄-顿辞谤补诲辞 et al., Journal of Biological Chemistry (2007) 282:24990-9
Molina et al., EMBO reports (2009) 10:246-51
笔茅谤别锄-顿辞谤补诲辞 et al., Nature Structural & Molecular Biology (2010) 17:576-81听听
Host: Aurora Martinez, Department of Biomedicine
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