Adenosine triphosphate(ATP)-binding cassette(ABC)transporter systems are divided into importers and exporters that facilitate the movement of diverse substrate molecules across the lipid bilayer,against the concentrat...Adenosine triphosphate(ATP)-binding cassette(ABC)transporter systems are divided into importers and exporters that facilitate the movement of diverse substrate molecules across the lipid bilayer,against the concentration gradient.These transporters comprise two highly conserved nucleotide-binding domains(NBDs)and two transmembrane domains(TMDs).Unlike ABC exporters,prokaryotic ABC importers require an additional substrate-binding protein(SBP)as a recognition site for specific substrate translocation.The discovery of a large number of ABC systems in bacterial pathogens revealed that these transporters are crucial for the establishment of bacterial infections.The existing literature has highlighted the roles of ABC transporters in bacterial growth,pathogenesis,and virulence.These roles include importing essential nutrients required for a variety of cellular processes and exporting outer membrane-associated virulence factors and antimicrobial substances.This review outlines the general structures and classification of ABC systems to provide a comprehensive view of the activities and roles of ABC transporters associated with bacterial virulence and pathogenesis during infection.展开更多
AB_(5)-type toxins are a group of secreted protein toxins that are central virulence factors for bacterial pathogens such as Shigella dysenteriae,Vibrio cholerae,Bordetella pertussis,and certain lineages of pathogenic...AB_(5)-type toxins are a group of secreted protein toxins that are central virulence factors for bacterial pathogens such as Shigella dysenteriae,Vibrio cholerae,Bordetella pertussis,and certain lineages of pathogenic Escherichia coli and Salmonella enterica.AB_(5) toxins are composed of an active(A)subunit that manipulates host cell biology in complex with a pentameric binding/delivery(B)subunit that mediates the toxin’s entry into host cells and its subsequent intracellular trafficking.Broadly speaking,all known AB_(5)-type toxins adopt similar structural architectures and employ similar mechanisms of binding,entering and trafficking within host cells.Despite this,there is a remarkable amount of diversity amongst AB_(5)-type toxins;this includes different toxin families with unrelated activities,as well as variation within families that can have profound functional consequences.In this review,we discuss the diversity that exists amongst characterized AB_(5)-type toxins,with an emphasis on the genetic and functional variability within AB_(5) toxin families,how this may have evolved,and its impact on human disease.展开更多
基金supported by the Universiti Kebangsaan Malaysia under the Research University Grant(No.GUP-2020-030)awarded to Sylvia CHIENG.
文摘Adenosine triphosphate(ATP)-binding cassette(ABC)transporter systems are divided into importers and exporters that facilitate the movement of diverse substrate molecules across the lipid bilayer,against the concentration gradient.These transporters comprise two highly conserved nucleotide-binding domains(NBDs)and two transmembrane domains(TMDs).Unlike ABC exporters,prokaryotic ABC importers require an additional substrate-binding protein(SBP)as a recognition site for specific substrate translocation.The discovery of a large number of ABC systems in bacterial pathogens revealed that these transporters are crucial for the establishment of bacterial infections.The existing literature has highlighted the roles of ABC transporters in bacterial growth,pathogenesis,and virulence.These roles include importing essential nutrients required for a variety of cellular processes and exporting outer membrane-associated virulence factors and antimicrobial substances.This review outlines the general structures and classification of ABC systems to provide a comprehensive view of the activities and roles of ABC transporters associated with bacterial virulence and pathogenesis during infection.
基金supported by a start-up grant provided by the Uni-versity of Alberta Faculty of Science(to C.C.F.)a Natural Sciences and Engineering Research Council of Canada(NSERC)Discovery Grant(Grant number:RGPIN-2020-03964 to C.C.F.).
文摘AB_(5)-type toxins are a group of secreted protein toxins that are central virulence factors for bacterial pathogens such as Shigella dysenteriae,Vibrio cholerae,Bordetella pertussis,and certain lineages of pathogenic Escherichia coli and Salmonella enterica.AB_(5) toxins are composed of an active(A)subunit that manipulates host cell biology in complex with a pentameric binding/delivery(B)subunit that mediates the toxin’s entry into host cells and its subsequent intracellular trafficking.Broadly speaking,all known AB_(5)-type toxins adopt similar structural architectures and employ similar mechanisms of binding,entering and trafficking within host cells.Despite this,there is a remarkable amount of diversity amongst AB_(5)-type toxins;this includes different toxin families with unrelated activities,as well as variation within families that can have profound functional consequences.In this review,we discuss the diversity that exists amongst characterized AB_(5)-type toxins,with an emphasis on the genetic and functional variability within AB_(5) toxin families,how this may have evolved,and its impact on human disease.
