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

Interspecies recombinational events during the evolution of altered PBP 2x genes in penicillin-resistant clinical isolates of Streptococcus pneumoniae.

Molecular microbiology - 1 Aug 1991

Laible G, Spratt B G, Hakenbeck R

Abstract excerpt

Penicillin resistance in pneumococci is due to the appearance of high molecular-weight penicillin-binding proteins (PBPs) that have reduced affinity for the antibiotic. We have compared the PBX 2x genes (pbpX) of one penicillin-susceptible and five penicillin-resistant clinical isolates of Streptococcus pneumoniae isolated from various parts of the world. All of the resistant isolates contained a low-affinity...

Read the complete abstract on PubMed

Topics

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

Share to Amino Acid Sequence
Share to Bacterial Proteins

Methodology Data sources Editorial policy Privacy Delete account & data About Contact Helena Bioinformatics

Share to Base Sequence

Share to Carrier Proteins

Share to Genetic Variation

Share to Molecular Sequence Data

Share to Sequence Homology, Nucleic Acid

Share to Species Specificity

Source

Identifiers

PMID: 1766375
DOI: 10.1111/j.1365-2958.1991.tb00821.x

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence. Graph snapshot: 2026-09-29.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Interspecies recombinational events during the evolution of altered PBP 2x genes in penicillin-resistant clinical isolates of Streptococcus pneumoniae.PMID 1766375Read ↗

Penicillin-binding proteins in Streptococcus pneumoniae: alterations during development of intrinsic penicillin resistance.Semantic proximity Read ↗

Five independent combinations of mutations can result in low-affinity penicillin-binding protein 2x of Streptococcus pneumoniae.Semantic proximity Read ↗

Evolution of penicillin resistance in Streptococcus pneumoniae; the role of Streptococcus mitis in the formation of a low affinity PBP2B in S. pneumoniae.Semantic proximity Read ↗

Genetic Heterogeneity in pbp Genes among Clinically Isolated Group B Streptococci with Reduced Penicillin SusceptibilitySemantic proximity Read ↗

Identical Penicillin-Binding Domains in Penicillin-Binding Proteins of <i>Streptococcus pneumoniae</i> Clinical Isolates with Different Levels of β-Lactam ResistanceSemantic proximity Read ↗

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

Interspecies recombination, not de novo mutation, maintains virulence after β-lactam resistance acquisition in Streptococcus pneumoniae.Semantic proximity Read ↗

Penicillin-resistant viridans streptococci have obtained altered penicillin-binding protein genes from penicillin-resistant strains of Streptococcus pneumoniae.Semantic proximity Read ↗

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

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

Molecular characteristics of penicillin-binding protein genes of penicillin-nonsusceptible Streptococcus pneumoniae isolated in the Netherlands.Semantic proximity Read ↗

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