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Alejandro Beceiro

Researcher at University of A Coruña

Publications -  72
Citations -  2968

Alejandro Beceiro is an academic researcher from University of A Coruña. The author has contributed to research in topics: Acinetobacter baumannii & Imipenem. The author has an hindex of 24, co-authored 62 publications receiving 2359 citations.

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Antimicrobial Resistance and Virulence: a Successful or Deleterious Association in the Bacterial World?

TL;DR: This review considers how bacterial virulence and fitness are affected by antibiotic resistance and also how the relationship between virulent and resistance is affected by different genetic mechanisms and by the most prevalent global responses.
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Biological Cost of Different Mechanisms of Colistin Resistance and Their Impact on Virulence in Acinetobacter baumannii

TL;DR: While Colistin resistance in A. baumannii confers a clear selective advantage in the presence of colistin treatment, it causes a noticeable cost in terms of overall fitness and virulence, with a more striking reduction associated with LPS loss than with phosphoethanolamine addition.
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Evaluation of different methods for detecting methicillin (oxacillin) resistance in Staphylococcus aureus

TL;DR: In the absence of availability of molecular biology techniques, the cefoxitin disc was the best predictor of methicillin resistance in S. aureus from among the techniques tested.
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Pan-β-Lactam Resistance Development in Pseudomonas aeruginosa Clinical Strains: Molecular Mechanisms, Penicillin-Binding Protein Profiles, and Binding Affinities

TL;DR: The results suggest that in addition to AmpC, efflux pumps, and OprD, the modification of PBP patterns appears to play a role in the in vivo emergence of PBLR strains, which still conserve certain susceptibility to the new antipseudomonal cephalosporin ceftolozane.
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Crystal structure of the carbapenemase OXA-24 reveals insights into the mechanism of carbapenem hydrolysis

TL;DR: The crystal structure of OXA-24 is determined and it is shown that the carbapenem's substrate specificity is determined by a hydrophobic barrier that is established through the specific arrangement of the Tyr-112 and Met-223 side chains, which define a tunnel-like entrance to the active site.