{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Rivera SL"],"funding":["American Cancer Society","Vetenskapsrådet","Knut och Alice Wallenbergs Stiftelse","National Institutes of Health","NIGMS NIH HHS","Kempe Foundation","National Science Foundation"],"pagination":["213-220.e4"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC7897265"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["28(2)"],"pubmed_abstract":["Transpeptidation reinforces the structure of cell-wall peptidoglycan, an extracellular heteropolymer that protects bacteria from osmotic lysis. The clinical success of transpeptidase-inhibiting β-lactam antibiotics illustrates the essentiality of these cross-linkages for cell-wall integrity, but the presence of multiple, seemingly redundant transpeptidases in many species makes it challenging to determine cross-link function. Here, we present a technique to link peptide strands by chemical rather than enzymatic reaction. We employ biocompatible click chemistry to induce triazole formation between azido- and alkynyl-d-alanine residues that are metabolically installed in the peptidoglycan of Gram-positive or Gram-negative bacteria. Synthetic triazole cross-links can be visualized using azido"],"journal":["Cell chemical biology"],"pubmed_title":["Chemically Induced Cell Wall Stapling in Bacteria."],"pmcid":["PMC7897265"],"funding_grant_id":["T32 GM120007","R25 GM086264"],"pubmed_authors":["Espaillat A","Shieh P","Aditham AK","Rivera SL","Kim J","Muriel-Mundo C","Cava F","Siegrist MS"],"additional_accession":[]},"is_claimable":false,"name":"Chemically Induced Cell Wall Stapling in Bacteria.","description":"Transpeptidation reinforces the structure of cell-wall peptidoglycan, an extracellular heteropolymer that protects bacteria from osmotic lysis. The clinical success of transpeptidase-inhibiting β-lactam antibiotics illustrates the essentiality of these cross-linkages for cell-wall integrity, but the presence of multiple, seemingly redundant transpeptidases in many species makes it challenging to determine cross-link function. Here, we present a technique to link peptide strands by chemical rather than enzymatic reaction. We employ biocompatible click chemistry to induce triazole formation between azido- and alkynyl-d-alanine residues that are metabolically installed in the peptidoglycan of Gram-positive or Gram-negative bacteria. Synthetic triazole cross-links can be visualized using azido","dates":{"release":"2021-01-01T00:00:00Z","publication":"2021 Feb","modification":"2025-04-04T02:25:08.968Z","creation":"2025-04-04T02:25:08.968Z"},"accession":"S-EPMC7897265","cross_references":{"pubmed":["33238158"],"doi":["10.1016/j.chembiol.2020.11.006"]}}