An abundance of bacterial ADP-ribosyltransferases - Implications for the origin of exotoxins and their human homologues

Mark J. Pallen; Alex C. Lam; Nicholas J. Loman; Alan McBride

doi:10.1016/S0966-842X(01)02074-1

An abundance of bacterial ADP-ribosyltransferases - Implications for the origin of exotoxins and their human homologues

Mark J. Pallen^*
, Alex C. Lam
, Nicholas J. Loman
, Alan McBride

^*Corresponding author for this work

Research output: Contribution to journal › Short survey › peer-review

64 Citations (Scopus)

Abstract

ADP-ribosylation is a post-translational modification that can be seen in many contexts, including as the primary mechanism of action of many important bacterial exotoxins. By data-mining complete and incomplete bacterial genome sequences, we have discovered >20 novel putative ADP-ribosyltransferases, including several new potential toxins.

Original language	English
Pages (from-to)	302-307
Number of pages	6
Journal	Trends in Microbiology
Volume	9
Issue number	7
DOIs	https://doi.org/10.1016/S0966-842X(01)02074-1
Publication status	Published - 1 Jul 2001
Externally published	Yes

Bibliographical note

Funding Information:
We thank the BBSRC for funding the ViruloGenome project. We gratefully acknowledge staff at the Sanger Centre, John Innes Centre, The Institute for Genomic Research, the University of Oklahoma and Genome Therapeutics for making incomplete genome sequence data publicly available.

UN SDGs

This output contributes to the following UN Sustainable Development Goals (SDGs)

SDG 3 Good Health and Well-being

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10.1016/S0966-842X(01)02074-1

Cite this

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title = "An abundance of bacterial ADP-ribosyltransferases - Implications for the origin of exotoxins and their human homologues",

abstract = "ADP-ribosylation is a post-translational modification that can be seen in many contexts, including as the primary mechanism of action of many important bacterial exotoxins. By data-mining complete and incomplete bacterial genome sequences, we have discovered >20 novel putative ADP-ribosyltransferases, including several new potential toxins.",

author = "Pallen, \{Mark J.\} and Lam, \{Alex C.\} and Loman, \{Nicholas J.\} and Alan McBride",

note = "Funding Information: We thank the BBSRC for funding the ViruloGenome project. We gratefully acknowledge staff at the Sanger Centre, John Innes Centre, The Institute for Genomic Research, the University of Oklahoma and Genome Therapeutics for making incomplete genome sequence data publicly available. ",

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T1 - An abundance of bacterial ADP-ribosyltransferases - Implications for the origin of exotoxins and their human homologues

AU - Pallen, Mark J.

AU - Lam, Alex C.

AU - Loman, Nicholas J.

AU - McBride, Alan

N1 - Funding Information: We thank the BBSRC for funding the ViruloGenome project. We gratefully acknowledge staff at the Sanger Centre, John Innes Centre, The Institute for Genomic Research, the University of Oklahoma and Genome Therapeutics for making incomplete genome sequence data publicly available.

PY - 2001/7/1

Y1 - 2001/7/1

N2 - ADP-ribosylation is a post-translational modification that can be seen in many contexts, including as the primary mechanism of action of many important bacterial exotoxins. By data-mining complete and incomplete bacterial genome sequences, we have discovered >20 novel putative ADP-ribosyltransferases, including several new potential toxins.

AB - ADP-ribosylation is a post-translational modification that can be seen in many contexts, including as the primary mechanism of action of many important bacterial exotoxins. By data-mining complete and incomplete bacterial genome sequences, we have discovered >20 novel putative ADP-ribosyltransferases, including several new potential toxins.

UR - https://www.scopus.com/pages/publications/0035400143

U2 - 10.1016/S0966-842X(01)02074-1

DO - 10.1016/S0966-842X(01)02074-1

M3 - Short survey

C2 - 11435081

AN - SCOPUS:0035400143

SN - 0966-842X

VL - 9

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EP - 307

JO - Trends in Microbiology

JF - Trends in Microbiology

IS - 7

ER -

An abundance of bacterial ADP-ribosyltransferases - Implications for the origin of exotoxins and their human homologues

Abstract

Bibliographical note

UN SDGs

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