Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

Two codependent routes lead to high-level MRSA.

Science (New York, N.Y.) - 1 Nov 2024

Adedeji-Olulana Abimbola Feyisara, Wacnik Katarzyna, Lafage Lucia, Pasquina-Lemonche Laia, Tinajero-Trejo Mariana, Sutton Joshua A F, Bilyk Bohdan, Irving Sophie E, Portman Ross Callum J, Meacock Oliver J, Randerson Sam A, Beattie Ewan, Owen David S, Florence James, Durham William M, Hornby David P, Corrigan Rebecca M, Green Jeffrey, Hobbs Jamie K, Foster Simon J

Abstract excerpt

Methicillin-resistant Staphylococcus aureus (MRSA), in which acquisition of mecA [which encodes the cell wall peptidoglycan biosynthesis component penicillin-binding protein 2a (PBP2a)] confers resistance to β-lactam antibiotics, is of major clinical concern. We show that, in the presence of antibiotics, MRSA adopts an alternative mode of cell division and shows an altered peptidoglycan architecture at the...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Anti-Bacterial Agents
Share to Bacterial Proteins

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Cell Division

Share to Cell Wall

Share to Methicillin Resistance

Share to Methicillin-Resistant Staphylococcus aureus

Share to Penicillin-Binding Proteins

Share to Peptidoglycan

Source

Identifiers

PMID: 39480932
DOI: 10.1126/science.adn1369

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 2 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Two codependent routes lead to high-level MRSA.PMID 39480932Read ↗

Altered PBP4 and GdpP functions synergistically mediate MRSA-like high-level, broad-spectrum β-lactam resistance in Staphylococcus aureus.Semantic proximity Read ↗

Beyond mecA: a two-tiered mechanism and regulatory rewiring drive high-level ceftaroline resistance in clinical MRSA.Semantic proximity Read ↗

A MRSA mystery: how PBP4 and cyclic-di-AMP join forces against β-lactam antibiotics.Semantic proximity Read ↗

Penicillin-Binding Protein 1 (PBP1) of Staphylococcus aureus Has Multiple Essential Functions in Cell DivisionSemantic proximity Read ↗

A PBP 2 mutant devoid of the transpeptidase domain abolishes spermine-β-lactam synergy in Staphylococcus aureus Mu50.Semantic proximity Read ↗

Methicillin Resistance in Staphylococcus Aureus: Mechanisms and ModulationSemantic proximity Read ↗

The Sle1 Cell Wall Amidase Is Essential for β-Lactam Resistance in Community-Acquired Methicillin-Resistant Staphylococcus aureus USA300Semantic proximity Read ↗

Ceftaroline is active against heteroresistant methicillin-resistant Staphylococcus aureus clinical strains despite associated mutational mechanisms and intermediate levels of resistance.Semantic proximity Read ↗

Evidence for a dual role of PBP1 in the cell division and cell separation of Staphylococcus aureus.Semantic proximity Read ↗

Mechanisms of Methicillin Resistance in <i>Staphylococcus aureus</i>Semantic proximity Read ↗

Molecular Bases Determining Daptomycin Resistance-Mediated Resensitization to β-Lactams (Seesaw Effect) in Methicillin-Resistant Staphylococcus aureus.Semantic proximity Read ↗

The basis for resistance to beta-lactam antibiotics by penicillin-binding protein 2a of methicillin-resistant Staphylococcus aureus.Semantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.