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2 an 23% sequence identity, the ectodomains in Visna and HIV-1 envelope glycoproteins show detailed str
3 scopy, we now visualize the functional maedi-visna lentivirus intasome at 4.9 angstrom resolution.
4 tif in a 10-amino-acid sequence derived from visna leukemia virus results in wild-type release of vir
5 sive pneumonia virus (OPPV) in the U.S., and Visna/Maedi virus (VMV) elsewhere, these viruses reduce
7 ere synthesized, and the soluble core of the Visna membrane fusion protein was reconstituted in solut
8 the cells examined were susceptible to MuLV/visna pseudotype viruses, supporting the notion that the
9 rs not only in cells classically infected by visna virus (i.e., macrophages and microglia), but also
10 The small-ruminant lentiviruses ovine maedi-visna virus (MVV) and caprine arthritis-encephalitis vir
11 m bovine immunodeficiency virus (BIV), maedi-visna virus (MVV) and equine infectious anemia virus (EI
15 protein (SU) gp135 of the lentiviruses maedi-visna virus and caprine arthritis-encephalitis virus (CA
16 s activators of two nonprimate lentiviruses, visna virus and equine infectious anemia virus, revealed
17 s), ERK-1/2, in primary cells susceptible to visna virus and report that virus infection induces and
18 itive, biologically relevant system to study visna virus cell entry and envelope-receptor interaction
19 type viruses, supporting the notion that the visna virus cellular receptor is a widely expressed prot
20 Based on those results, additional HIV-1/visna virus chimeric integrases were designed and purifi
21 alpha- and gamma-retroviruses, and the maedi visna virus dimer linkage region is capable of forming h
22 virus (MuLV) particles pseudotyped with the visna virus envelope glycoprotein and encoding a green f
23 re obtained when the cytoplasmic tail of the visna virus envelope TM protein was truncated to 3, 7, o
24 s of human immunodeficiency virus type 1 and visna virus guided the quantitative testing of oligonucl
27 substitutions at the analogous positions in visna virus integrase and Rous sarcoma virus integrase c
35 n interactions with cellular proteins at the visna virus promoter, we used an in vitro protein affini
40 inhibitor of the ERK/MAPK pathway, abolishes visna virus replication, as evidenced by extremely low l
41 cells not considered to be major targets of visna virus replication, suggesting that activation of t
42 at proximal to the viral TATA box, where the visna virus Tat activation domain could contact TBP to a
48 n in vivo two-hybrid assay, to show that the visna virus Tat protein specifically interacts with the
50 ike other lentiviral transactivators such as visna virus Tat, is unable to transactivate from minimal
51 from human immunodeficiency virus type 1 and visna virus were able to substitute for the EIAV slipper
52 unodeficiency virus, Jembrana disease virus, visna virus, and caprine arthritis encephalitis virus.
53 ases of human immunodeficiency virus type 1, visna virus, and Rous sarcoma virus exhibited different
54 ns of human immuno- deficiency virus type 1, visna virus, and Rous sarcoma virus exhibited distinct p
56 of ERK-1/2 activation in brains derived from visna virus-infected sheep demonstrates a strong correla
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