Discover Community Create You

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

A PBP2x from a clinical isolate of Streptococcus pneumoniae exhibits an alternative mechanism for reduction of susceptibility to beta-lactam antibiotics.

The Journal of biological chemistry - 16 Apr 2004

Pernot Lucile, Chesnel Laurent, Le Gouellec Audrey, Croizé Jacques, Vernet Thierry, Dideberg Otto, Dessen Andréa

Abstract excerpt

The human pathogen Streptococcus pneumoniae is one of the main causative agents of respiratory tract infections. At present, clinical isolates of S. pneumoniae often exhibit decreased susceptibility toward beta-lactams, a phenomenon linked to multiple mutations within the penicillin-binding prote...

Read the complete abstract on PubMed

Topics

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

Share to beta-Lactam Resistance
Share to Binding Sites
Share to Carrier Proteins

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Models, Molecular

Share to Penicillin-Binding Proteins

Share to Protein Conformation

Share to Ribonucleoproteins

Share to Streptococcus pneumoniae

Source

Identifiers

PMID: 14734544
DOI: 10.1074/jbc.M313492200

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 4 Sept 2026. Prepared record publication-14734544-2026-09-04.2. Manifest publication-graph-cohort-2026-09-04.2.

Source receipt: PubMed via Helena Literature Corpus, retrieved 4 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

A PBP2x from a clinical isolate of Streptococcus pneumoniae exhibits an alternative mechanism for reduction of susceptibility to beta-lactam antibiotics.PMID 14734544Read ↗

Pneumococcal beta-lactam resistance due to a conformational change in penicillin-binding protein 2x.Semantic proximity Read ↗

The crystal structure of the penicillin-binding protein 2x from Streptococcus pneumoniae and its acyl-enzyme form: implication in drug resistance.Semantic proximity Read ↗

Crystal structure of PBP2x from a highly penicillin-resistant Streptococcus pneumoniae clinical isolate: a mosaic framework containing 83 mutations.Semantic proximity Read ↗

The structural modifications induced by the M339F substitution in PBP2x from Streptococcus pneumoniae further decreases the susceptibility to beta-lactams of resistant strains.Semantic proximity Read ↗

Mutations in the active site of penicillin-binding protein PBP2x from Streptococcus pneumoniae. Role in the specificity for beta-lactam antibiotics.Semantic proximity Read ↗

Reduced In Vitro Susceptibility of Streptococcus pyogenes to β-Lactam Antibiotics Associated with Mutations in the pbp2x Gene Is Geographically Widespread.Semantic proximity Read ↗

Penicillin-binding proteins 2x and 2b as primary PBP targets in Streptococcus pneumoniae.Semantic proximity Read ↗

Crystal structure of penicillin-binding protein 1a (PBP1a) reveals a mutational hotspot implicated in beta-lactam resistance in Streptococcus pneumoniae.Semantic proximity Read ↗

Molecular analysis of pbp2b in Streptococcus pneumonia isolated from clinical and normal flora samples.Semantic proximity Read ↗

Biochemical characterization of Streptococcus pneumoniae penicillin-binding protein 2b and its implication in beta-lactam resistance.Semantic proximity Read ↗

Identification of a structural determinant for resistance to β-lactam antibiotics in Gram-positive bacteriaSemantic proximity Read ↗

Insight into the Diversity of Penicillin-Binding Protein 2x Alleles and Mutations in Viridans Streptococci.Semantic proximity Read ↗

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