Izolace a charakteristika proteinu p12 Mason-Pfizerova opičího viru

Kód výsledku v IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F60461373%3A22330%2F04%3A00012824" target="_blank" >RIV/60461373:22330/04:00012824 - isvavai.cz</a>

Výsledek na webu

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DOI - Digital Object Identifier

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Jazyk výsledku

angličtina

Název v původním jazyce

Isolation and characterization of the Mason-Pfizer monkey virus p12 protein

Popis výsledku v původním jazyce

The Mason#Pfizer monkey virus (M-PMV) Gag protein, precursor to the structural proteins of the infectious virion, assembles intoimmature capsid-like particles when expressed at high levels in bacterial cells. Similar capsid-like particles can be obtainedby in vitroassembly using a high concentration of isolated Gag. M-PMV Gag contains a p12 protein that has no corresponding analogues in most otherretroviruses and has been suggested to contain an internal scaffold domain (ISD). We have expressed and purified p12 and the N- and Cterminalhalves (Np12 and Cp12) that are predicted to be structurally independent domains. The behavior of these proteins was analyzedusing chemical cross-linking, CD spectroscopy, and electron microscopy. The N-terminal half ofp12 is largely a-helical although the Cterminalportion lacks any apparent ordered structure. Both p12 and Np12 form high-order oligomers in vitro and when expressed in E. coliproduce organized structures that are visible by electron micro

Název v anglickém jazyce

Isolation and characterization of the Mason-Pfizer monkey virus p12 protein

Popis výsledku anglicky

The Mason#Pfizer monkey virus (M-PMV) Gag protein, precursor to the structural proteins of the infectious virion, assembles intoimmature capsid-like particles when expressed at high levels in bacterial cells. Similar capsid-like particles can be obtainedby in vitroassembly using a high concentration of isolated Gag. M-PMV Gag contains a p12 protein that has no corresponding analogues in most otherretroviruses and has been suggested to contain an internal scaffold domain (ISD). We have expressed and purified p12 and the N- and Cterminalhalves (Np12 and Cp12) that are predicted to be structurally independent domains. The behavior of these proteins was analyzedusing chemical cross-linking, CD spectroscopy, and electron microscopy. The N-terminal half ofp12 is largely a-helical although the Cterminalportion lacks any apparent ordered structure. Both p12 and Np12 form high-order oligomers in vitro and when expressed in E. coliproduce organized structures that are visible by electron micro

Druh

J_x - Nezařazeno - Článek v odborném periodiku (Jimp, Jsc a Jost)

CEP obor

CE - Biochemie

OECD FORD obor

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Projekt

<a href="/cs/project/LN00A079" target="_blank" >LN00A079: Centrum integrované genomiky</a><br>

Návaznosti

P - Projekt vyzkumu a vyvoje financovany z verejnych zdroju (s odkazem do CEP)

Rok uplatnění

2004

Kód důvěrnosti údajů

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

Název periodika

Virology

ISSN

0947-6539

e-ISSN

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Svazek periodika

2004

Číslo periodika v rámci svazku

324

Stát vydavatele periodika

BE - Belgické království

Počet stran výsledku

9

Strana od-do

204-212

Kód UT WoS článku

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EID výsledku v databázi Scopus

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