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@ARTICLE{Kumari2026-kr,
  title     = "A non-canonical, moonlighting Acinetobacter baumannii
               glyceraldehyde-3-phosphate dehydrogenase ({GAPDH/GapA}) promotes
               iron acquisition from heme, transferrin and lactoferrin",
  author    = "Kumari, Anjali and Gani, Zahid and Ramesh, Nimma and Gaikwad,
               Shreya and Kumar, Ajay and Dilawari, Rahul and Mahajan, Apurwa
               and Rohilla, Rajesh Kumar and Kumaran, Sangaralingam and Raje,
               Manoj and Raje, Chaaya Iyengar",
  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 ∼150 kDa homo-tetramer, composed of ∼37 kDa monomers. The
               present study reveals that A. baumannii expresses an unusually
               large enzyme of ∼212 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.",
  journal   = "Biochimie",
  publisher = "Elsevier BV",
  volume    =  245,
  pages     = "55--71",
  month     =  jun,
  year      =  2026,
  keywords  = "Acinetobacter baumannii (A. baumannii); Entner-doudoroff
               pathway; Glyceraldehyde-3-phosphate dehydrogenase (GAPDH); Iron;
               Protein multifunctionality",
  language  = "en"
}