Role of Mason-Pfizer Monkey Virus CA-NC Spacer Peptide-Like Domain in Assembly of Immature Particles

0437896 - ÚOCHB 2015 RIV US eng J - Článek v odborném periodiku
Strohalmová-Böhmová, Karolína - Spiwok, V. - Lepšík, Martin - Hadravová, Romana - Křížová, Ivana - Ulbrich, P. - Pichová, Iva - Bednárová, Lucie - Ruml, T. - Rumlová, Michaela
Role of Mason-Pfizer Monkey Virus CA-NC Spacer Peptide-Like Domain in Assembly of Immature Particles.
Journal of Virology. Roč. 88, č. 24 (2014), s. 14148-14160. ISSN 0022-538X. E-ISSN 1098-5514
Grant CEP: GA ČR(CZ) GA14-15326S; GA MŠMT LO1302; GA ČR GBP208/12/G016
Institucionální podpora: RVO:61388963
Klíčová slova: human immunodeficiency virus * HIV-1 capsid protein * murine leukemia virus
Kód oboru RIV: EE - Mikrobiologie, virologie
Impakt faktor: 4.439, rok: 2014

The hexameric lattice of an immature retroviral particle consists of Gag polyprotein, which is the precursor of all viral structural proteins. Lentiviral and alpharetroviral Gag proteins contain a peptide sequence called the spacer peptide (SP), which is localized between the capsid (CA) and nucleocapsid (NC) domains. SP plays a critical role in intermolecular interactions during the assembly of immature particles of several retroviruses. Published models of supramolecular structures of immature particles suggest that in lentiviruses and alpharetroviruses, SP adopts a rod-like six-helix bundle organization. In contrast, Mason-Pfizer monkey virus (M-PMV), a betaretrovirus that assembles in the cytoplasm, does not contain a distinct SP sequence, and the CA-NC connecting region is not organized into a clear rod-like structure. Nevertheless, the CA-NC junction comprises a sequence critical for assembly of immature M-PMV particles. In the present work, we characterized this region, called the SP-like domain, in detail. We provide biochemical data confirming the critical role of the MPMV SP-like domain in immature particle assembly, release, processing, and infectivity. Circular dichroism spectroscopy revealed that, in contrast to the SP regions of other retroviruses, a short SP-like domain-derived peptide (SPLP) does not form a purely helical structure in aqueous or helix-promoting solution. Using 8-angstrom cryo-electron microscopy density maps of immature M-PMV particles, we prepared computational models of the SP-like domain and indicate the structural features required for M-PMV immature particle assembly.
Trvalý link: http://hdl.handle.net/11104/0241378