Difference between revisions of "Part:BBa K404152"
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| + | <h3>General informations</h3> | ||
| + | Whereas VP1 is translated from the minor spliced mRNA, while VP2 and VP3 are translated from the major spliced mRNA. The minor spliced product is approximately 10-fold less abundant than the major spliced mRNA. Thus, there is much less VP1 than VP2 and VP3 resulting in a capsid stoichiometric ratio of 1:1:10. The N terminus of VP1 has an extension of 65 amino acids including an additional extension of 138 N-terminal amino acids forming the unique portion of VP1. It contains a motif of about 70 amino acids that is highly homologous to phospholipase A2 (PLA2) domain. Furthermore, there are nuclear localization sequences (BR)(+), which are supposed to be necessary for endosomal escape and nuclear entry. (Bleker, Pawlita, & Kleinschmidt, 2006), (DiPrimio, Asokan, Govindasamy, Agbandje-McKenna, & Samulski, 2008), (Johnson et al., 2010a) | ||
| + | <h3>VP1up</h3> | ||
VP1up protein is a derivate of Vp1 protein, which contains several point mutations that lead to significant decrease in enzymatic activity of phospholipase. Phospholipase is located on N terminus in VP1 [Canaan et al., 2004; Zadori et al., 2001], which is required for virus internalisation [Girod et al., 2002] | VP1up protein is a derivate of Vp1 protein, which contains several point mutations that lead to significant decrease in enzymatic activity of phospholipase. Phospholipase is located on N terminus in VP1 [Canaan et al., 2004; Zadori et al., 2001], which is required for virus internalisation [Girod et al., 2002] | ||
Revision as of 13:36, 27 October 2010
[AAV2]-VP1up
General informations
Whereas VP1 is translated from the minor spliced mRNA, while VP2 and VP3 are translated from the major spliced mRNA. The minor spliced product is approximately 10-fold less abundant than the major spliced mRNA. Thus, there is much less VP1 than VP2 and VP3 resulting in a capsid stoichiometric ratio of 1:1:10. The N terminus of VP1 has an extension of 65 amino acids including an additional extension of 138 N-terminal amino acids forming the unique portion of VP1. It contains a motif of about 70 amino acids that is highly homologous to phospholipase A2 (PLA2) domain. Furthermore, there are nuclear localization sequences (BR)(+), which are supposed to be necessary for endosomal escape and nuclear entry. (Bleker, Pawlita, & Kleinschmidt, 2006), (DiPrimio, Asokan, Govindasamy, Agbandje-McKenna, & Samulski, 2008), (Johnson et al., 2010a)
VP1up
VP1up protein is a derivate of Vp1 protein, which contains several point mutations that lead to significant decrease in enzymatic activity of phospholipase. Phospholipase is located on N terminus in VP1 [Canaan et al., 2004; Zadori et al., 2001], which is required for virus internalisation [Girod et al., 2002]
Sequence and Features
- 10COMPATIBLE WITH RFC[10]
- 12COMPATIBLE WITH RFC[12]
- 21INCOMPATIBLE WITH RFC[21]Illegal XhoI site found at 28
Illegal XhoI site found at 214 - 23COMPATIBLE WITH RFC[23]
- 25COMPATIBLE WITH RFC[25]
- 1000COMPATIBLE WITH RFC[1000]
References
Canaan, 2004. Interfacial enzymology of parvovirus phospholipases A2. The Journal of Biological Chemistry, 279(15), pp.14502-14508.
Girod, A., 2002. The VP1 capsid protein of adeno-associated virus type 2 is carrying a phospholipase A2 domain required for virus infectivity. The Journal of general virology, 83(Pt 5), pp.973-978. Available at: http://www.ncbi.nlm.nih.gov/pubmed/11961250.
Zadori, Z , 2001. A viral phospholipase A2 is required for parvovirus infectivity. Developmental Cell, 1(2), pp.291-302. Available at: http://www.ncbi.nlm.nih.gov/pubmed/11702787.