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Related Concept Videos

Single Nucleotide Polymorphisms-SNPs01:05

Single Nucleotide Polymorphisms-SNPs

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A single nucleotide polymorphism or SNP is a single nucleotide variation at a specific genomic position in a large population. It is the most prevalent type of sequence variation found in the human genome. Point mutations that occur in more than 1% of the population qualify as SNPs. These are present once every 1000 nucleotides on an average in the human genome. Replacement of a purine with another purine (A/G) or a pyrimidine with another pyrimidine (C/T) is known as a transition. In contrast,...
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Conserved Binding Sites01:49

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Many proteins’ biological role depends on their interactions with their ligands, small molecules that bind to specific locations on the protein known as ligand-binding sites. Ligand-binding sites are often conserved among homologous proteins as these sites are critical for protein function.
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For successful DNA replication, the unwinding of double-stranded DNA must be accompanied by stabilization and protection of the separated single strands of the DNA. This crucial task is performed by single-strand DNA-binding (SSB) proteins. They bind to the DNA in a sequence-independent manner, which means that the nitrogenous bases of the DNA need not be present in a specific order for binding of SSB proteins to it. The binding of SSB proteins straightens single-stranded DNA (ssDNA) and makes...
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Development of Antibiotic Resistance01:30

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Antibiotic resistance is a major public health concern that arises when bacteria evolve mechanisms to withstand the effects of antibiotic treatments. This resistance can be intrinsic, acquired through genetic mutations, or transferred between bacteria via horizontal gene transfer. The development of antibiotic resistance poses significant challenges in treating bacterial infections and necessitates ongoing research to develop new therapeutic strategies.Intrinsic resistance occurs when bacterial...
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Comparing Copy Number Variations and SNPs02:26

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Sequencing of the human genome has opened up several best-kept secrets of the genome. Scientists have identified thousands of genome variations that exist within a population. These variations can be a single nucleotide or a larger chromosomal variation.
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Updated: Dec 23, 2025

Constructing Mutants in Serotype 1 Streptococcus pneumoniae strain 519/43
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Constructing Mutants in Serotype 1 Streptococcus pneumoniae strain 519/43

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Restricted Sequence Variation in Streptococcus pyogenes Penicillin Binding Proteins.

Andrew Hayes1, Jake A Lacey2, Jacqueline M Morris1

  • 1Department of Microbiology and Immunology, University of Melbourne, Peter Doherty Institute for Infection and Immunity, Melbourne, Victoria, Australia.

Msphere
|May 1, 2020
PubMed
Summary
This summary is machine-generated.

Penicillin binding protein (PBP) mutations conferring beta-lactam resistance are rare in Streptococcus pyogenes, unlike in Streptococcus pneumoniae. This suggests strong constraints limit PBP variation in S. pyogenes, maintaining low resistance rates.

Keywords:
Streptococcus pyogenesbeta-lactamspenicillin binding proteinspenicillin resistance

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Area of Science:

  • Microbiology and Infectious Diseases
  • Genomics and Molecular Biology
  • Antimicrobial Resistance

Background:

  • Beta-lactam antibiotics are primary treatments for Streptococcus pyogenes infections.
  • Recent reports identified beta-lactam resistance in S. pyogenes linked to penicillin binding protein (PBP) mutations, raising concerns.
  • Penicillin binding protein mutations are common in Streptococcus pneumoniae, contributing to their beta-lactam resistance.

Purpose of the Study:

  • To investigate the prevalence of penicillin binding protein (PBP) sequence variation in Streptococcus pyogenes globally.
  • To determine if mutations conferring reduced beta-lactam susceptibility are widespread in S. pyogenes.
  • To compare PBP mutation frequency in S. pyogenes with that in S. pneumoniae.

Main Methods:

  • Analysis of a global database containing 9,667 Streptococcus pyogenes isolates.
  • Sequencing and comparative analysis of key penicillin binding proteins (PBP2x, PBP1a, PBP1b, PBP2a).
  • Comparison with 2,520 Streptococcus pneumoniae sequences.

Main Results:

  • Penicillin binding protein mutations are infrequent in the global S. pyogenes population, with minimal amino acid variation.
  • Only 4 out of 9,667 S. pyogenes strains had mutations near the active sites of PBP2x or PBP1a.
  • The specific PBP2x T553K substitution linked to resistance was not found; PBP mutations are significantly less common than in S. pneumoniae.

Conclusions:

  • Extensive, uncharacterized constraints likely limit penicillin binding protein sequence plasticity in Streptococcus pyogenes.
  • Despite antibiotic pressure, mutations conferring beta-lactam resistance are not becoming fixed or sequentially acquired in S. pyogenes.
  • Findings support the rarity of beta-lactam resistance in S. pyogenes and suggest limited potential for widespread resistance development via PBP mutations.