Počet záznamů: 1
Bordetella Pertussis Adenylate Cyclase Toxin Does Not Possess a Phospholipase A Activity, Serine 606 and Aspartate 1079 Residues Are Not Involved in Target Cell Delivery of the Adenylyl Cyclase Enzyme Domain
- 1.
SYSNO ASEP 0491750 Druh ASEP J - Článek v odborném periodiku Zařazení RIV J - Článek v odborném periodiku Poddruh J Článek ve WOS Název Bordetella Pertussis Adenylate Cyclase Toxin Does Not Possess a Phospholipase A Activity, Serine 606 and Aspartate 1079 Residues Are Not Involved in Target Cell Delivery of the Adenylyl Cyclase Enzyme Domain Tvůrce(i) Bumba, Ladislav (MBU-M) RID, ORCID
Mašín, Jiří (MBU-M) RID, ORCID
Osičková, Adriana (MBU-M) RID, ORCID
Osička, Radim (MBU-M) RID, ORCID
Šebo, Peter (MBU-M) RID, ORCIDČíslo článku 245 Zdroj.dok. Toxins. - : MDPI - ISSN 2072-6651
Roč. 10, č. 6 (2018)Poč.str. 11 s. Jazyk dok. eng - angličtina Země vyd. CH - Švýcarsko Klíč. slova adenylate cyclase toxin ; phospholipase A activity ; AC domain translocation Vědní obor RIV EE - Mikrobiologie, virologie Obor OECD Microbiology CEP GA16-05919S GA ČR - Grantová agentura ČR GA18-20621S GA ČR - Grantová agentura ČR LM2015064 GA MŠMT - Ministerstvo školství, mládeže a tělovýchovy NV16-28126A GA MZd - Ministerstvo zdravotnictví Institucionální podpora MBU-M - RVO:61388971 UT WOS 000436131800033 EID SCOPUS 85048723920 DOI 10.3390/toxins10060245 Anotace The adenylate cyclase toxin-hemolysin (CyaA, ACT, or AC-Hly) plays a crucial role in virulence and airway colonization capacity of the whooping cough agent Bordetella pertussis. The toxin penetrates target cell membranes and exhibits three distinct biological activities. A population of CyaA conformers forms small cation-selective pores that permeabilize the cell membrane for potassium efflux, which can provoke colloid-osmotic (oncotic) cell lysis. The other two activities are due to CyaA conformers that transiently form calcium influx conduits in the target cell membrane and translocate the adenylate cyclase (AC) enzyme into cytosol of cells. A fourth putative biological activity has recently been reported, an intrinsic phospholipase A (PLA) activity was claimed to be associated with the CyaA polypeptide and be involved in the mechanism of translocation of the AC enzyme polypeptide across cell membrane lipid bilayer. However, the conclusions drawn by the authors contradicted their own results and we show them to be erroneous. We demonstrate that highly purified CyaA is devoid of any detectable phospholipase A1 activity and that contrary to the published claims, the two putative conserved phospholipase A catalytic residues, namely the Ser606 and Asp1079 residues, are not involved in the process of membrane translocation of the AC domain of CyaA across target membranes. Pracoviště Mikrobiologický ústav Kontakt Eliška Spurná, eliska.spurna@biomed.cas.cz, Tel.: 241 062 231 Rok sběru 2019
Počet záznamů: 1