title: Molecular aspects and comparative genomics of bacteriophage endolysins.
abstract: Phages are recognized as the most abundant and diverse entities on the planet. Their diversity is determined predominantly by their dynamic adaptation capacities when confronted with different selective pressures in an endless cycle of coevolution with a widespread group of bacterial hosts. At the end of the infection cycle, progeny virions are confronted with a rigid cell wall that hinders their release into the environment and the opportunity to start a new infection cycle. Consequently, phages encode hydrolytic enzymes, called endolysins, to digest the peptidoglycan. In this work, we bring to light all phage endolysins found in completely sequenced double-stranded nucleic acid phage genomes and uncover clues that explain the phage-endolysin-host ecology that led phages to recruit unique and specialized endolysins.
authors: Institute for Biotechnology and Bioengineering, Centre of Biological Engineering, University of Minho, Campus de Gualtar, Braga, Portugal.
authors: Hugo
authors: H
authors: Oliveira
authors: Luís D R
authors: LD
authors: Melo
authors: Sílvio B
authors: SB
authors: Santos
authors: Franklin L
authors: FL
authors: Nóbrega
authors: Eugénio C
authors: EC
authors: Ferreira
authors: Nuno
authors: N
authors: Cerca
authors: Joana
authors: J
authors: Azeredo
authors: Leon D
authors: LD
authors: Kluskens
mesh_terms: D001435:Bacteriophages / Q000201:enzymology*; D019295:Computational Biology; D010450:Endopeptidases / Q000235:genetics* / Q000378:metabolism*; D006868:Hydrolysis; D010457:Peptidoglycan / Q000378:metabolism; D010802:Phylogeny; D017386:Sequence Homology, Amino Acid; D014764:Viral Proteins / Q000235:genetics / Q000378:metabolism
chemical_list: D010457:Peptidoglycan; D014764:Viral Proteins; D010450:Endopeptidases; C001143:endolysin