mADP-RTs: Versatile virulence factors from bacterial pathogens of plants and mammals

• Main Authors: Lennart eWirthmueller, Mark J. Banfield
• Format: Article
• Language: English
• Published: Frontiers Media S.A. 2012-06-01
• Series: Frontiers in Plant Science
• Subjects: crystal structure; mono-ADP-ribosyltransferase; pathogen effector; plant innate immunity; effector crystal structure; mono-ADP-ribosylation
• Online Access: http://journal.frontiersin.org/Journal/10.3389/fpls.2012.00142/full

Mono ADP-ribosyltransferases (mADP-RTs) are a family of enzymes that cleave NAD+ and covalently attach the ADP-ribosyl moiety to target proteins. mADP-RTs are well established as important virulence factors of bacteria that infect mammals. Cholera toxin, pertussis toxin and diphteria toxin are three of the best-known examples of mADP-RTs. They modify host target proteins in order to promote infection and/or killing of the host cell. Despite low sequence similarity at the primary amino acid level, mADP-RTs share a conserved core catalytic fold and structural biology has made important contributions to elucidating how mADP-RTs modify mammalian host targets. Recently, mADP-RTs were shown to be present in plant pathogenic bacteria, suggesting that mADP-RTs are also important virulence factors of plant pathogens. Crystal structures of plant pathogenic bacterial mADP-RTs are also now available. Here we review the structure/function of mADP-RTs from pathogens of mammals and plants, highlighting both commonalities and differences.