Peptidoglycan Endopeptidase from Novel Adaiavirus Bacteriophage Lyses Pseudomonas aeruginosa Strains as Well as Arthrobacter globiformis and A. pascens Bacteria

. 2023 Jul 26 ; 11 (8) : . [epub] 20230726

Status PubMed-not-MEDLINE Jazyk angličtina Země Švýcarsko Médium electronic

Typ dokumentu časopisecké články

Perzistentní odkaz   https://www.medvik.cz/link/pmid37630448

Grantová podpora
RVO60077344 Czech Academy of Sciences
Strategie AV 21 Czech Academy of Sciences
LM2012062 MEYS CR
CZ.02.1.01/0.0/0.0/16_013/0001775 ERDF

Odkazy

PubMed 37630448
PubMed Central PMC10458142
DOI 10.3390/microorganisms11081888
PII: microorganisms11081888
Knihovny.cz E-zdroje

A novel virus lytic for Pseudomonas aeruginosa has been purified. Its viral particles have a siphoviral morphology with a head 60 nm in diameter and a noncontractile tail 184 nm long. The dsDNA genome consists of 16,449 bp, has cohesive 3' termini, and encodes 28 putative proteins in a single strain. The peptidoglycan endopeptidase encoded by ORF 16 was found to be the lytic enzyme of this virus. The recombinant, purified enzyme was active up to 55 °C in the pH range 6-9 against all tested isolates of P. aeruginosa, but, surprisingly, also against the distant Gram-positive micrococci Arthrobacter globiformis and A. pascens. Both this virus and its endolysin are further candidates for possible treatment against P. aeruginosa and probably also other bacteria.

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