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Original title:
Studium skládání a pučení částic viru myšího tumoru prsní žlázy MMTV
Translated title: Study of the assembly and budding of mouse mammary tumor virus MMTV
Authors: Hoboth, Peter ; Zábranský, Aleš (advisor) ; Forstová, Jitka (referee)
Document type: Master’s theses
Year: 2009
Language: slo
Abstract: Mouse mammary tumor virus (MMTV) is a prototypical member of the Betaretrovirus genus characterized by the ability to preassemble viral particles in the cytoplasm of the host cells. Intracellularly preassembled particles are subsequently transported to the plasma membrane being enveloped by a lipid bilayer and released from the cell in the process referred to as budding. Retrovirus particle assembly is driven by the Gag polyprotein precursor, which is cleaved in the maturation process by virus-encoded protease to liberate multiple structural proteins. The matrix (MA), capsid (CA) and nucleocapsid (NC) protein domains that are common to all retroviruses and in the case of MMTV, also the noncanonical domains, pp21, p3, p8 and "n", located between MA and CA domain are present. The role of these specific domains remains undefined. The retroviral budding is stimulated by short peptide motifs, so-called late (L) domains, located within Gag sequence. These L domains mediate interactions with cellular proteins normally involved in the biogenesis of the multivesicular bodies and protein sorting. Three types of the L domains have been identified to date, with the consensus of the amino acid sequences (i) P(T/S)AP, (ii) YP(x)nL (where x represents any amino acid and n≤3) and (iii) PPxY. Disruption of the L domain...
Institution: Charles University Faculties (theses) (web)
Document availability information: Available in the Charles University Digital Repository.
Original record: http://hdl.handle.net/20.500.11956/25357
Permalink: http://www.nusl.cz/ntk/nusl-485185
The record appears in these collections:
Universities and colleges > Public universities > Charles University > Charles University Faculties (theses)
Academic theses (ETDs) > Master’s theses
Translated title: Study of the assembly and budding of mouse mammary tumor virus MMTV
Authors: Hoboth, Peter ; Zábranský, Aleš (advisor) ; Forstová, Jitka (referee)
Document type: Master’s theses
Year: 2009
Language: slo
Abstract: Mouse mammary tumor virus (MMTV) is a prototypical member of the Betaretrovirus genus characterized by the ability to preassemble viral particles in the cytoplasm of the host cells. Intracellularly preassembled particles are subsequently transported to the plasma membrane being enveloped by a lipid bilayer and released from the cell in the process referred to as budding. Retrovirus particle assembly is driven by the Gag polyprotein precursor, which is cleaved in the maturation process by virus-encoded protease to liberate multiple structural proteins. The matrix (MA), capsid (CA) and nucleocapsid (NC) protein domains that are common to all retroviruses and in the case of MMTV, also the noncanonical domains, pp21, p3, p8 and "n", located between MA and CA domain are present. The role of these specific domains remains undefined. The retroviral budding is stimulated by short peptide motifs, so-called late (L) domains, located within Gag sequence. These L domains mediate interactions with cellular proteins normally involved in the biogenesis of the multivesicular bodies and protein sorting. Three types of the L domains have been identified to date, with the consensus of the amino acid sequences (i) P(T/S)AP, (ii) YP(x)nL (where x represents any amino acid and n≤3) and (iii) PPxY. Disruption of the L domain...
Institution: Charles University Faculties (theses) (web)
Document availability information: Available in the Charles University Digital Repository.
Original record: http://hdl.handle.net/20.500.11956/25357
Permalink: http://www.nusl.cz/ntk/nusl-485185
The record appears in these collections:
Universities and colleges > Public universities > Charles University > Charles University Faculties (theses)
Academic theses (ETDs) > Master’s theses
Record created 2022-05-08, last modified 2022-05-08