Benfang Lei's research on heme acquisition in Gram-positive pathogens and bacterial pathogenesi

来源 :World Journal of Biological Chemistry | 被引量 : 0次 | 上传用户:xuzw93
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Benfang Lei’s laboratory conducts research on pathogenesis of human pathogen Group A Streptococcus (GAS)and horse pathogen Streptococcus equi(S.equi). His current research focuses on heme acquisition in Gram-positive pathogens and molecular mechanism of GAS and S.equi pathogenesis.Heme is an important source of essential iron for bacterial pathogens.Benfang Lei and colleagues identified the first cell surface heme-binding protein in Gram-positive pathogens and the heme acquisition system in GAS,demonstrated direct heme transfer from one protein to another,demonstrated an experimental pathway of heme acquisition by the Staphylococcus aureus Isd system,elucidated the activated heme transfer mechanism,and obtained evidence for a chemical mechanism of direct axial ligand displacement during the Shp-to-HtsA heme transfer reaction.These findings have considerably contributed to the progress that has been made over recent years in understanding the heme acquisition process in Grampositive pathogens.Pathogenesis of GAS is mediated by an abundance of extracellular proteins,and pathogenic role and functional mechanism are not known for many of these virulence factors.Lei laboratory identified a secreted protein of GAS as a CovRS-regulated virulence factor that is a protective antigen and is critical for GAS spreading in the skin and systemic dissemination.These studies may lead to development of novel strategies to prevent and treat GAS infections. Benfang Lei’s laboratory conducts research on pathogenesis of human pathogen Group A Streptococcus (GAS) and horse pathogen Streptococcus equi (S..equi). His current research focuses on heme acquisition in Gram-positive pathogens and molecular mechanism of GAS and S..equi pathogenesis. Heme is an important source of essential iron for bacterial pathogens. Benfang Lei and colleagues identified the first cell surface heme-binding protein in Gram-positive pathogens and the heme acquisition system in GAS, demonstrated direct heme transfer from one protein to another, demonstrated an experimental pathway of heme acquisition by the Staphylococcus aureus Isd system, and elucidated the activated heme transfer mechanism, and obtained evidence for a chemical mechanism of direct axial ligand displacement during the Shp-to-HtsA heme transfer reaction. the findings have substantial contributed to the progress that has been made over recent years in understanding the heme acquisition process in Grampositive pat hogens. Pathogenesis of GAS is mediated by an abundance of extracellular proteins, and pathogenic role and functional mechanisms are not known for many of these virulence factors. Lei laboratory identified a secreted protein of GAS as a CovRS-regulated virulence factor that is a protective antigen and is critical for GAS spreading in the skin and systemic dissemination. These studies may lead to development of novel strategies to prevent and treat GAS infections.
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