madp-rts: versatile virulence factors from bacterial pathogens of plants and mammals

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ID: 235296
2012
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Abstract
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.
Reference Key
ewirthmueller2012frontiersmadp-rts: Use this key to autocite in the manuscript while using SciMatic Manuscript Manager or Thesis Manager
Authors ;Lennart eWirthmueller;Mark J. Banfield
Journal phytochemistry letters
Year 2012
DOI
10.3389/fpls.2012.00142
URL
http://journal.frontiersin.org/Journal/10.3389/fpls.2012.00142/full
Keywords
crystal structure mono-adp-ribosylationplant culture

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