Structural highlights
Function
[HA11_MOUSE] Involved in the presentation of foreign antigens to the immune system. [GLYC_LYCVA] Stable signal peptide (SSP) is cleaved but is apparently retained as the third component of the GP complex. The SSP is required for efficient glycoprotein expression, post-translational cleavage of GP1 and GP2, glycoprotein transport to the cell plasma membrane, formation of infectious virus particles, and acid pH-dependent glycoprotein-mediated cell fusion.[1] Glycoprotein G1 mediates virus attachment to host receptor alpha-dystroglycan DAG1. This attachment induces virion internalization predominantly through clathrin- and caveolin-independent endocytosis.[2] Glycoprotein G2 is a class I viral fusion protein, that directs fusion of viral and host endosomal membranes, leading to delivery of the nucleocapsid into the cytoplasm. Membrane fusion is mediated by irreversable conformational changes induced upon acidification in the endosome.[3] [B2MG_MOUSE] Component of the class I major histocompatibility complex (MHC). Involved in the presentation of peptide antigens to the immune system.
References
- ↑ Saunders AA, Ting JP, Meisner J, Neuman BW, Perez M, de la Torre JC, Buchmeier MJ. Mapping the landscape of the lymphocytic choriomeningitis virus stable signal peptide reveals novel functional domains. J Virol. 2007 Jun;81(11):5649-57. Epub 2007 Mar 21. PMID:17376927 doi:http://dx.doi.org/10.1128/JVI.02759-06
- ↑ Cao W, Henry MD, Borrow P, Yamada H, Elder JH, Ravkov EV, Nichol ST, Compans RW, Campbell KP, Oldstone MB. Identification of alpha-dystroglycan as a receptor for lymphocytic choriomeningitis virus and Lassa fever virus. Science. 1998 Dec 11;282(5396):2079-81. PMID:9851928
- ↑ Di Simone C, Zandonatti MA, Buchmeier MJ. Acidic pH triggers LCMV membrane fusion activity and conformational change in the glycoprotein spike. Virology. 1994 Feb;198(2):455-65. PMID:8291229 doi:http://dx.doi.org/10.1006/viro.1994.1057
