Characterization of the Interface of the Bone Marrow Stromal Cell Antigen 2–Vpu Protein Complex via Computational Chemistry

Biochemistry ◽  
2012 ◽  
Vol 51 (6) ◽  
pp. 1288-1296 ◽  
Author(s):  
Jinming Zhou ◽  
Zhixin Zhang ◽  
Zeyun Mi ◽  
Xin Wang ◽  
Quan Zhang ◽  
...  
2019 ◽  
Vol 4 (7) ◽  
pp. S50-S51
Author(s):  
T. INOUE ◽  
J. Yao ◽  
L. Huang ◽  
D. Rosin ◽  
K. Ishihara ◽  
...  

2015 ◽  
Vol 11 (1) ◽  
Author(s):  
Valentina Franceschi ◽  
Antonio Capocefalo ◽  
Sarah Jacca ◽  
Alfonso Rosamilia ◽  
Sandro Cavirani ◽  
...  

2015 ◽  
Vol 7 (11) ◽  
pp. 2427-2435 ◽  
Author(s):  
Mohammed Fayez Al Rez ◽  
H. Fouad ◽  
Ezzedine Laourine ◽  
Martin Hild ◽  
Dilbar Aibibu ◽  
...  

Gene ◽  
2018 ◽  
Vol 661 ◽  
pp. 133-138
Author(s):  
Jiawen Wang ◽  
Shuai Bian ◽  
Meichun Liu ◽  
Xin Zhang ◽  
Siming Wang ◽  
...  

1999 ◽  
Vol 337 (3) ◽  
pp. 491-496 ◽  
Author(s):  
Atsushi SATO ◽  
Sumie YAMAMOTO ◽  
Katsuhiko ISHIHARA ◽  
Toshio HIRANO ◽  
Hisato JINGAMI

cADP-ribose, which is produced by ecto-ADP-ribosyl cyclase of CD38 or bone marrow stromal cell antigen-1 (BST-1), is a key regulator of Ca2+-induced calcium release in an Ins(1,4,5)P3-independent manner. In the present study, we have identified a specific peptide inhibitor for ADP-ribosyl cyclase of BST-1. A 15-mer random peptide phage library was screened with a soluble form of BST-1 expressed in baculovirus-infected insect cells. After biopanning, two potent sequences reactive towards BST-1 were isolated. The two synthetic peptides corresponding to the identified sequences were shown to antagonize each other's ability to inhibit the binding of the two isolated phage to BST-1, suggesting that they bind at a common binding site on BST-1. One of the peptides (SNP-1) was shown to inhibit ADP-ribosyl cyclase activity of BST-1 in an uncompetitive manner with a Ki value of 180±40 nM (n = 3). SNP-1 also inhibited cyclic ADP-ribose hydrolase activity of BST-1 dose-dependently. Selected phage did not cross-react with a soluble form of CD38. SNP-1 did not show any inhibitory effect on ADP-ribosyl cyclase activity of CD38, and therefore this peptide inhibitor will be useful to serve as a starting tool for understanding the roles of these intriguing ecto-enzymes. This is the first report of a specific ADP-ribosyl cyclase inhibitor.


2010 ◽  
Vol 84 (9) ◽  
pp. 4415-4425 ◽  
Author(s):  
Frederick Arnaud ◽  
Sarah G. Black ◽  
Lita Murphy ◽  
David J. Griffiths ◽  
Stuart J. Neil ◽  
...  

ABSTRACT Endogenous betaretroviruses (enJSRVs) of sheep are expressed abundantly in the female reproductive tract and play a crucial role in conceptus development and placental morphogenesis. Interestingly, the colonization of the sheep genome by enJSRVs is likely still ongoing. During early pregnancy, enJSRV expression correlates with the production of tau interferon (IFNT), a type I IFN, by the developing conceptus. IFNT is the pregnancy recognition signal in ruminants and possesses potent antiviral activity. In this study, we show that IFNT induces the expression of bone marrow stromal cell antigen 2 (BST2) (also termed CD317/tetherin) both in vitro and in vivo. The BST2 gene is duplicated in ruminants. Transfection assays found that ovine BST2 proteins (oBST2A and oBST2B) block release of viral particles produced by intact enJSRV loci and of related exogenous and pathogenic jaagsiekte sheep retrovirus (JSRV). Ovine BST2A appears to restrict enJSRVs more efficiently than oBST2B. In vivo, the expression of BST2A/B and enJSRVs in the endometrium increases after day 12 and remains high between days 14 and 20 of pregnancy. In situ hybridization analyses found that oBST2A is expressed mainly in the endometrial stromal cells but not in the luminal and glandular epithelial cells, in which enJSRVs are highly expressed. In conclusion, enJSRVs may have coevolved in the presence of oBST2A/B by being expressed in different cellular compartments of the same organ. Viral expression in cells unable to express BST2 may be one of the mechanisms used by retroviruses to escape restriction.


2016 ◽  
Vol 35 (3) ◽  
pp. 172-176 ◽  
Author(s):  
Ning Kong ◽  
Qiong Meng ◽  
Yongguang Wu ◽  
Zhongze Wang ◽  
Yewen Zuo ◽  
...  

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