The Role of properdin in killing of non-pathogenic Leptospira biflexa

Full metadata record
DC FieldValueLanguage
dc.contributorLab. Bacteriologiapt_BR
dc.contributorCentro Bioindustrialpt_BR
dc.contributor.authorMartinez, Adriana Patricia Granadospt_BR
dc.contributor.authorAbreu, Patricia Antonia Estimapt_BR
dc.contributor.authorVasconcellos, Silvio de Arrudapt_BR
dc.contributor.authorHo, Paulo Leept_BR
dc.contributor.authorFerreira, Viviana P.pt_BR
dc.contributor.authorSaggu, Gurpannapt_BR
dc.contributor.authorBarbosa, Angela Silvapt_BR
dc.contributor.authorIsaac, Lourdespt_BR
dc.identifier.citationMartinez APG, Abreu PAE, Vasconcellos SA, Lee Ho P, Ferreira VP., Saggu G, et al. The Role of properdin in killing of non-pathogenic Leptospira biflexa. Front. Immunol.. 2020 Nov;11:572562. doi:10.3389/fimmu.2020.572562.pt_BR
dc.description.abstractProperdin (P) is a positive regulatory protein that stabilizes the C3 convertase and C5 convertase of the complement alternative pathway (AP). Several studies have suggested that properdin can bind directly to the surface of certain pathogens regardless of the presence of C3bBb. Saprophytic Leptospira are susceptible to complement-mediated killing, but the interaction of properdin with Leptospira spp. has not been evaluated so far. In this work, we demonstrate that properdin present in normal human serum, purified properdin, as well as properdin oligomers P2, P3, and P4, interact with Leptospira. Properdin can bind directly to the bacterial surface even in the absence of C3b. In line with our previous findings, AP activation was shown to be important for killing non-pathogenic L. biflexa, and properdin plays a key role in this process since this microorganism survives in P-depleted human serum and the addition of purified properdin to P-depleted human serum decreases the number of viable leptospires. A panel of pathogenic L. interrogans recombinant proteins was used to identify putative properdin targets. Lsa30, an outer membrane protein from L. interrogans, binds to unfractionated properdin and to a lesser extent to P2-P4 properdin oligomers. In conclusion, properdin plays an important role in limiting bacterial proliferation of non-pathogenic Leptospira species. Once bound to the leptospiral surface, this positive complement regulatory protein of the AP contributes to the formation of the C3 convertase on the leptospire surface even in the absence of prior addition of C3b.pt_BR
dc.description.sponsorship(FAPESP) Fundação de Amparo à Pesquisa do Estado de São Paulopt_BR
dc.description.sponsorship(CNPq) Conselho Nacional de Desenvolvimento Científico e Tecnológicopt_BR
dc.relation.ispartofFrontiers in Immunologypt_BR
dc.rightsOpen accesspt_BR
dc.titleThe Role of properdin in killing of non-pathogenic Leptospira biflexapt_BR
dc.rights.licenseCC BYpt_BR
dc.contributor.external(USP) Universidade de São Paulopt_BR
dc.contributor.externalUniversity of Toledopt_BR
dc.subject.keywordcomplement systempt_BR
dc.subject.keywordalternative pathwaypt_BR
dc.subject.keywordbacteria killing abilitypt_BR
dc.relation.ispartofabbreviatedFront Immunolpt_BR
dc.identifier.citationabntv. 11, 572562, nov. 2020pt_BR
dc.identifier.citationvancouver2020 Nov;11:572562pt_BR
dc.contributor.butantanAbreu, Patricia Antonia Estima|:Pesquisador|:Lab. Bacteriologiapt_BR
dc.contributor.butantanHo, Paulo Lee|:Pesquisador|:Centro Bioindustrialpt_BR
dc.contributor.butantanBarbosa, Angela Silva|:Pesquisador|:Lab. Bacteriologiapt_BR
dc.sponsorship.butantan(FAPESP) Fundação de Amparo à Pesquisa do Estado de São Paulo¦¦2017/12924-3pt_BR
dc.sponsorship.butantan(FAPESP) Fundação de Amparo à Pesquisa do Estado de São Paulo¦¦2012/23708-6pt_BR
dc.sponsorship.butantan(CNPq) Conselho Nacional de Desenvolvimento Científico e Tecnológico¦¦141874/2012-0pt_BR
item.fulltextCom Texto completo-
Appears in Collections:Artigos de periódicos

Files in This Item:

Size: 821.82 kB
Format: Adobe PDF
Show simple item record

This item is licensed under a Creative Commons License Creative Commons