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primary topic: A non-canonical, moonlighting Acinetobacter baumannii glyceraldehyde-3-phosphate dehydrogenase (GAPDH/GapA) promotes iron acquisition from heme, transferrin and lactoferrin

A non-canonical, moonlighting Acinetobacter baumannii glyceraldehyde-3-phosphate dehydrogenase (GAPDH/GapA) promotes iron acquisition from heme, transferrin and lactoferrin
type: AcademicArticle
type: Article
abstract: Acinetobacter baumannii (A. baumannii) has emerged a priority pathogen due the rapid spread of multi-drug resistant strains. Despite this, a number of metabolic pathways of this pathogen remain uncharacterized and are inferred from studies in E. coli. Whole genome analysis of clinical isolates of A. baumannii revealed the absence of several glycolytic enzymes, however, all enzymes of the Entner-Doudoroff (ED) pathway were identified, but none are characterized. Moreover, two products of this pathway i.e. glyceraldehyde-3-phosphate (G3P) and pyruvate generate deoxyxylulose 5-phosphate which is a key intermediate of Vitamin B6 synthesis. Glyceraldehyde-3-phosphate dehydrogenase (GAPDH) is highly conserved across species and despite sequence differences the functional enzyme is most often a â�¼150 kDa homo-tetramer, composed of â�¼37 kDa monomers. The present study reveals that A. baumannii expresses an unusually large enzyme of â�¼212 kDa, with a monomer size of 53 kDa. The A. baumannii enzyme differs due to the presence of a unique N-terminal extension of 396 bp corresponding to 132 amino acids. Sequence analysis revealed that this N-terminal sequence is present across several Acinetobacter species. Our study provides the complete biochemical characterization of recombinant GapA. In addition, we identified that GapA sequesters and internalizes human transferrin (Tf), lactoferrin (Lf) and heme as an effective mechanism for iron acquisition by the pathogen. Considering its pivotal role in carbon metabolism, vitamin B6 synthesis and iron acquisition, A. baumannii GapA could significantly contribute to bacterial pathogenesis. Further, its unique structural differences may provide an opportunity for development of specific inhibitors.
date: 2026-06-10
volume: 245
status: peerReviewed
status: published
author list: authors
type: EPrint
type: ArticleEPrint
is part of: repository
has document: A non-canonical, moonlighting Acinetobacter baumannii glyceraldehyde-3-phosphate dehydrogenase (GAPDH/GapA) promotes iron acquisition from heme, transferrin and lactoferrin (HTML)
subject: QR Microbiology

A non-canonical, moonlighting Acinetobacter baumannii glyceraldehyde-3-phosphate dehydrogenase (GAPDH/GapA) promotes iron acquisition from heme, transferrin and lactoferrin (HTML)
type: Document
has file: references (2).bib
has part: references (2).bib

Elsevier BV
type: Organization

Biochimie
type: Collection

Chaaya Iyengar Raje
type: Person
given name: Chaaya Iyengar
family name: Raje

Shreya Gaikwad
type: Person
given name: Shreya
family name: Gaikwad

Anjali Kumari
type: Person
given name: Anjali
family name: Kumari

Manoj Raje
type: Person
given name: Manoj
family name: Raje

Rahul Dilawari
type: Person
given name: Rahul
family name: Dilawari

Nimma Ramesh
type: Person
given name: Nimma
family name: Ramesh

Sangaralingam Kumaran
type: Person
given name: Sangaralingam
family name: Kumaran

Zahid Gani
type: Person
given name: Zahid
family name: Gani

Ajay Kumar
type: Person
given name: Ajay
family name: Kumar

Apurwa Mahajan
type: Person
given name: Apurwa
family name: Mahajan

Rajesh Kumar Rohilla
type: Person
given name: Rajesh Kumar
family name: Rohilla

HTML Summary of #3482 A non-canonical, moonlighting Acinetobacter baumannii glyceraldehyde-3-phosphate dehydrogenase (GAPDH/GapA) promotes iron acquisition from heme, transferrin and lactoferrin
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primary topic: A non-canonical, moonlighting Acinetobacter baumannii glyceraldehyde-3-phosphate dehydrogenase (GAPDH/GapA) promotes iron acquisition from heme, transferrin and lactoferrin

QR Microbiology
type: Concept