Acylation of Lysine 860 Allows Tight Binding and Cytotoxicity of Bordetella Adenylate Cyclase on CD1 1b-Expressing Cells

Result code in IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F61388971%3A_____%2F05%3A00022198" target="_blank" >RIV/61388971:_____/05:00022198 - isvavai.cz</a>

Alternative codes found

RIV/00216208:11310/05:00008377 RIV/00216208:11310/05:8377

Result on the web

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DOI - Digital Object Identifier

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Result language

angličtina

Original language name

Acylation of Lysine 860 Allows Tight Binding and Cytotoxicity of Bordetella Adenylate Cyclase on CD1 1b-Expressing Cells

Original language description

The Bordetella adenylate cyclase toxin-hemolysin (CyaA, ACT, or AC-Hly) forms cation-selective membrane channels and delivers into the cytosol of target cells an adenylate cyclase domain (AC) that catalyzes uncontrolled conversion of cellular ATP to cAMP. Both toxin activities were previously shown to depend on post-translational activation of proCyaA to CyaA by covalent palmitoylation of the internal Lys983 residue (K983). CyaA, however, harbors a second RTX acylation site at residue Lys860 (K860), andthe role of K860 acylation in toxin activity is unclear

Czech name

Acylace lysinového zbytku 860 umožňuje pevnou vazbu a cytotoxickou aktivitu adenylát-cyklazového toxinu baktérie Bordetella pertussis na buňkách exprimunjících CD11b

Czech description

Práce ukazuje, že jediná acylace jak na lysinu 860 tak na lysinu 983 postačuje pro těsnou interakci ACT s integrinovým receptorem CD11b/CD18. Tato funkční redundance dvou acylačních míst nemá zřejmý důvod, nicméně umožňuje průnik toxinu do buněk přes plasmatickou membránu

Type

J_x - Unclassified - Peer-reviewed scientific article (Jimp, Jsc and Jost)

CEP classification

EE - Microbiology, virology

OECD FORD branch

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Project

Result was created during the realization of more than one project. More information in the Projects tab.

Continuities

P - Projekt vyzkumu a vyvoje financovany z verejnych zdroju (s odkazem do CEP)<br>Z - Vyzkumny zamer (s odkazem do CEZ)

Publication year

2005

Confidentiality

S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů

Name of the periodical

Biochemistry

ISSN

0006-2960

e-ISSN

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Volume of the periodical

44

Issue of the periodical within the volume

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Country of publishing house

US - UNITED STATES

Number of pages

7

Pages from-to

12766-12759

UT code for WoS article

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EID of the result in the Scopus database

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