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Interdimer Interactions Between Alph...

Towell, Brian B.

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Interdimer Interactions Between Alphavirus E1 And E2 Glycoprtoeins Display Host Dependence in Spike Assembly.

紀錄類型:	書目-電子資源 : Monograph/item
正題名/作者:	Interdimer Interactions Between Alphavirus E1 And E2 Glycoprtoeins Display Host Dependence in Spike Assembly./
作者:	Towell, Brian B.
出版者:	Ann Arbor : ProQuest Dissertations & Theses, : 2017,
面頁冊數:	82 p.
附註:	Source: Masters Abstracts International, Volume: 56-04.
Contained By:	Masters Abstracts International56-04(E).
標題:	Biochemistry. -
電子資源:	http://pqdd.sinica.edu.tw/twdaoapp/servlet/advanced?query=10235187
ISBN:	9781369770629

Interdimer Interactions Between Alphavirus E1 And E2 Glycoprtoeins Display Host Dependence in Spike Assembly.
Towell, Brian B.

Interdimer Interactions Between Alphavirus E1 And E2 Glycoprtoeins Display Host Dependence in Spike Assembly. - Ann Arbor : ProQuest Dissertations & Theses, 2017 - 82 p.

Source: Masters Abstracts International, Volume: 56-04.

Thesis (M.S.)--Indiana University, 2017.

A virus must identify a potential host, insert the viral genetic material into the host, generating new viral proteins and viral genomes, and assembling the aforementioned components into complete viral particles that can exit and infect another host to generate future progeny. Assembly of these particles can be complex and coordinates multiples molecules. In an alphavirus, assembly of the spike complex is critical for success of future virus progeny.

ISBN: 9781369770629Subjects--Topical Terms:

518028
Biochemistry.

Interdimer Interactions Between Alphavirus E1 And E2 Glycoprtoeins Display Host Dependence in Spike Assembly.
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520 $a The alphavirus spike is made up of three E1-E2 heterodimers. E2 is critical for host-receptor binding and entry, while E1 is critical for viral membrane fusion with the host endosome to deposit the positively stranded viral genome into the host cytoplasm. Once the genome is translated, E1 and E2 must properly fold, assemble into a dimer, then spike complex. This complex must translocate to the plasma membrane to participate in budding and exit where it gains a viral envelope from the host membrane. Work has demonstrated that interactions between E1 and E2 are critical for dimer assembly, and future function of the viral spike. Little work has investigated potential interactions between dimers within a spike. In this study, we utilized structural data to identify resides between the E1 glycoprotein and the E2 glycoprotein of adjacent dimers within an alphavirus spike, that we hypothesize to be important in alphavirus spike function. Our evidence demonstrates that these "piggy-back" residues, are important for the proper function and assembly of the alphavirus spike, and that there are potential differences in assembly between an arthropod host and a mammalian host.
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