Work

NAD+-dependent post-translational modification of Escherichia coli glyceraldehyde-3-phosphate dehydrogenase.

Year: 2009

Type: article

Abstract: Glyceraldehyde-3-phosphate dehydrogenase (GAPDH) is a multifunctional housekeeping protein reported to be a target of several covalent modifications in many organisms. In a previous study, enterohemorrhagic (EHEC) and enteropathogenic (EPEC) Escherichia coli strains were shown to secrete GAPDH and the protein to bind human plasminogen and fibrinogen. Here we report that GAPDH of these pathogens is ADP-ribosylated either in the cytoplasm or in the extracellular medium. GAPDH catalyzes its own modification, which involves Cys-149 at the active site. ADP-ribosylation of extracellular GAPDH may play an important role in the host-pathogen interaction, as also proposed in other pathogens.

Source: PubMed

Authors: Laura Aguilera, Rosa Giménez, Josefa Badia, Juan Aguilar, Laura Baldoma

Institutions: Institut de Biomedicina de la Universitat de Barcelona, Universitat de Barcelona

Language: English

Topic: Escherichia coli research studies

Subfield: Microbiology

Field: Immunology and Microbiology

Domain: Life Sciences

SDG: Good health and well-being

Open Access status: green

Funder: Ministerio de Economía y Competitividad

OpenAlex ID: W2152602329

FWCI: 1.517

Cites: 18

Cited by: 17

Related to: 10