A Secreted NlpC/P60 Endopeptidase from Photobacterium damselae subsp. piscicida Cleaves the Peptidoglycan of Potentially Competing Bacteria

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MetadadosDescriçãoIdioma
Autor(es): dc.contributorUniv Porto-
Autor(es): dc.contributorInst Pasteur-
Autor(es): dc.contributorINSERM Grp Avenir-
Autor(es): dc.contributorCNRS-
Autor(es): dc.contributorCSIC-
Autor(es): dc.contributorUniv Santiago de Compostela-
Autor(es): dc.contributorUniversidade Estadual Paulista (Unesp)-
Autor(es): dc.creatorLisboa, Johnny-
Autor(es): dc.creatorPereira, Cassilda-
Autor(es): dc.creatorRifflet, Aline-
Autor(es): dc.creatorAyala, Juan-
Autor(es): dc.creatorTerceti, Mateus S. [UNESP]-
Autor(es): dc.creatorBarca, Alba V.-
Autor(es): dc.creatorRodrigues, Ines-
Autor(es): dc.creatorBarbosa Pereira, Pedro Jose-
Autor(es): dc.creatorOsorio, Carlos R.-
Autor(es): dc.creatorGarcia-del Portillo, Francisco-
Autor(es): dc.creatorBoneca, Ivo Gomperts-
Autor(es): dc.creatorVale, Ana do-
Autor(es): dc.creatorSantos, Nuno M. S. dos-
Data de aceite: dc.date.accessioned2022-02-22T00:59:27Z-
Data de disponibilização: dc.date.available2022-02-22T00:59:27Z-
Data de envio: dc.date.issued2021-06-25-
Data de envio: dc.date.issued2021-06-25-
Data de envio: dc.date.issued2020-12-31-
Fonte completa do material: dc.identifierhttp://dx.doi.org/10.1128/mSphere.00736-20-
Fonte completa do material: dc.identifierhttp://hdl.handle.net/11449/210307-
Fonte: dc.identifier.urihttp://educapes.capes.gov.br/handle/11449/210307-
Descrição: dc.descriptionPeptidoglycan (PG) is a major component of the bacterial cell wall, forming a mesh-like structure enwrapping the bacteria that is essential for maintaining structural integrity and providing support for anchoring other components of the cell envelope. PG biogenesis is highly dynamic and requires multiple enzymes, including several hydrolases that cleave glycosidic or amide bonds in the PG. This work describes the structural and functional characterization of an NlpC/P60-containing peptidase from Photobacterium damselae subsp. piscicida (Phdp), a Gram-negative bacterium that causes high mortality of warm-water marine fish with great impact for the aquaculture industry. PnpA (Photobacterium NlpC-like protein A) has a four-domain structure with a hydrophobic and narrow access to the catalytic center and specificity for the gamma-D-glutamyl-meso-diaminopimelic acid bond. However, PnpA does not cleave the PG of Phdp or PG of several Gram-negative and Gram-positive bacterial species. Interestingly, it is secreted by the Phdp type II secretion system and degrades the PG of Vibrio anguillarum and Vibrio vulnificus. This suggests that PnpA is used by Phdp to gain an advantage over bacteria that compete for the same resources or to obtain nutrients in nutrient-scarce environments. Comparison of the muropeptide composition of PG susceptible and resistant to the catalytic activity of PnpA showed that the global content of muropeptides is similar, suggesting that susceptibility to PnpA is determined by the three-dimensional organization of the muropeptides in the PG. IMPORTANCE Peptidoglycan (PG) is a major component of the bacterial cell wall formed by long chains of two alternating sugars interconnected by short peptides, generating a mesh-like structure that enwraps the bacterial cell. Although PG provides structural integrity and support for anchoring other components of the cell envelope, it is constantly being remodeled through the action of specific enzymes that cleave or join its components. Here, it is shown that Photobacterium damselae subsp. piscicida, a bacterium that causes high mortality in warm-water marine fish, produces PnpA, an enzyme that is secreted into the environment and is able to cleave the PG of potentially competing bacteria, either to gain a competitive advantage and/or to obtain nutrients. The specificity of PnpA for the PG of some bacteria and its inability to cleave others may be explained by differences in the structure of the PG mesh and not by different muropeptide composition.-
Descrição: dc.descriptionFundo Europeu de Desenvolvimento Regional (FEDER) funds through the COMPETE 2020 Operacional Program for Competitiveness and Internationalization (POCI), Portugal 2020-
Descrição: dc.descriptionPortuguese funds through Fundacao para a Ciencia e a Tecnologia/Ministerio da Ciencia, Tecnologia e Ensino Superior (FCT)-
Descrição: dc.descriptionFundacao para a Ciencia e a Tecnologia (FCT), I.P.-
Descrição: dc.descriptionState Agency for Research (AEI) of Spain-
Descrição: dc.descriptionFEDER Program from the European Union-
Descrição: dc.descriptionFrench Government's Investissement d'Avenir program, Laboratoire d'Excellence Integrative Biology of Emerging Infectious Diseases-
Descrição: dc.descriptionLaboratoire d'Excellence Integrative Biology of Emerging Infectious Diseases-
Descrição: dc.descriptionInfec-ERA grant-
Descrição: dc.descriptionUniv Porto, Inst Biol Mol & Celular IBMC, Fish Immunol & Vaccinol Grp, Porto, Portugal-
Descrição: dc.descriptionUniv Porto, Inst Invest & Inovacao Saude I3S, Fish Immunol & Vaccinol Grp, Porto, Portugal-
Descrição: dc.descriptionInst Pasteur, Unite Biol & Genet Paroi Bacterienne, Paris, France-
Descrição: dc.descriptionINSERM Grp Avenir, Paris, France-
Descrição: dc.descriptionCNRS, UMR Integrated & Mol Microbiol, Paris, France-
Descrição: dc.descriptionCSIC, Ctr Biol Mol Severo Ochoa CBMSO, Madrid, Spain-
Descrição: dc.descriptionUniv Santiago de Compostela, Inst Acuicultura, Dept Microbiol & Parasitol, Santiago De Compostela, Spain-
Descrição: dc.descriptionUniv Porto, Inst Biol Mol & Celular IBMC, Biomol Struct Grp, Porto, Portugal-
Descrição: dc.descriptionUniv Porto, Inst Invest & Inovacao Saude I3S, Macromol Struct Grp, Porto, Portugal-
Descrição: dc.descriptionCSIC, Ctr Nacl Biotecnol CNB, Lab Patogenos Bacterianos Intracelulares, Madrid, Spain-
Descrição: dc.descriptionUniv Porto, Stem Cells Regenerat Biol & Repair, Inst Nacl Engn Biomed INEB, Porto, Portugal-
Descrição: dc.descriptionUniv Porto, Inst Invest & Inovacao Saude I3S, Porto, Portugal-
Descrição: dc.descriptionUniv Estadual Paulista ENESP, Dept Biol Geral & Aplicada, Inst Biociencias Rio Claro Sao Paulo, Sao Paulo, Brazil-
Descrição: dc.descriptionUniv Estadual Paulista ENESP, Dept Biol Geral & Aplicada, Inst Biociencias Rio Claro Sao Paulo, Sao Paulo, Brazil-
Descrição: dc.descriptionPortuguese funds through Fundacao para a Ciencia e a Tecnologia/Ministerio da Ciencia, Tecnologia e Ensino Superior (FCT): POCI-01-0145-FEDER-030018 (PTDC/CVT-CVT/30018/2017)-
Descrição: dc.descriptionFundacao para a Ciencia e a Tecnologia (FCT), I.P.: DL57/2016/CP1355/CT0010-
Descrição: dc.descriptionFEDER Program from the European Union: AGL2016-79738-R-
Descrição: dc.descriptionFEDER Program from the European Union: BIO2016-77639-P-
Descrição: dc.descriptionFrench Government's Investissement d'Avenir program, Laboratoire d'Excellence Integrative Biology of Emerging Infectious Diseases: ANR10-LABX-62-IBEID-
Descrição: dc.descriptionInfec-ERA grant: 16-IFEC-0004-03-
Formato: dc.format23-
Idioma: dc.languageen-
Publicador: dc.publisherAmer Soc Microbiology-
Relação: dc.relationMsphere-
???dc.source???: dc.sourceWeb of Science-
Palavras-chave: dc.subjectNlpC/P60-
Palavras-chave: dc.subjectVibrio anguillarum-
Palavras-chave: dc.subjectVibrio vulnificus-
Palavras-chave: dc.subjectX-ray crystallography-
Palavras-chave: dc.subjectcell wall hydrolases-
Palavras-chave: dc.subjectpeptidoglycan-
Palavras-chave: dc.subjectPhotobacterium damselae subsp. piscicida-
Palavras-chave: dc.subjecttype II secretion system-
Título: dc.titleA Secreted NlpC/P60 Endopeptidase from Photobacterium damselae subsp. piscicida Cleaves the Peptidoglycan of Potentially Competing Bacteria-
Tipo de arquivo: dc.typelivro digital-
Aparece nas coleções:Repositório Institucional - Unesp

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