Henderson L E, Sowder R, Smythers G, Benveniste R E, Oroszlan S
J Virol. 1985 Sep;55(3):778-87. doi: 10.1128/JVI.55.3.778-787.1985.
A new D-type retrovirus originally designated SAIDS-D/Washington and here referred to as retrovirus-D/Washington (R-D/W) was recently isolated at the University of Washington Primate Center, Seattle, Wash., from a rhesus monkey with an acquired immunodeficiency syndrome and retroperitoneal fibromatosis. To better establish the relationship of this new D-type virus to the prototype D-type virus, Mason-Pfizer monkey virus (MPMV), we have purified and compared six structural proteins from each virus. The proteins purified from each D-type retrovirus include p4, p10, p12, p14, p27, and a phosphoprotein designated pp18 for MPMV and pp20 for R-D/W. Amino acid analysis and N-terminal amino acid sequence analysis show that the p4, p12, p14, and p27 proteins of R-D/W are distinct from the homologous proteins of MPMV but that these proteins from the two different viruses share a high degree of amino acid sequence homology. The p10 proteins from the two viruses have similar amino acid compositions, and both are blocked to N-terminal Edman degradation. The phosphoproteins from the two viruses each contain phosphoserine but are different from each other in amino acid composition, molecular weight, and N-terminal amino acid sequence. The data thus show that each of the R-D/W proteins examined is distinguishable from its MPMV homolog and that a major difference between these two D-type retroviruses is found in the viral phosphoproteins. The N-terminal amino acid sequences of D-type retroviral proteins were used to search for sequence homologies between D-type and other retroviral amino acid sequences. An unexpected amino acid sequence homology was found between R-D/W pp20 (a gag protein) and a 28-residue segment of the env precursor polyprotein of Rous sarcoma virus. The N-terminal amino acid sequences of the D-type major gag protein (p27) and the nucleic acid-binding protein (p14) show only limited amino acid sequence homology to functionally homologous proteins of C-type retroviruses.
一种最初命名为SAIDS - D/华盛顿、此处称为逆转录病毒 - D/华盛顿（R - D/W）的新型D型逆转录病毒，最近在华盛顿大学灵长类动物中心（位于华盛顿州西雅图）从一只患有获得性免疫缺陷综合征和腹膜后纤维瘤病的恒河猴体内分离出来。为了更好地确定这种新型D型病毒与原型D型病毒——梅森 - 辉瑞猴病毒（MPMV）之间的关系，我们对每种病毒的六种结构蛋白进行了纯化和比较。从每种D型逆转录病毒中纯化得到的蛋白包括p4、p10、p12、p14、p27，以及一种磷蛋白，MPMV的该磷蛋白命名为pp18，R - D/W的命名为pp20。氨基酸分析和N端氨基酸序列分析表明，R - D/W的p4、p12、p14和p27蛋白与MPMV的同源蛋白不同，但这两种不同病毒的这些蛋白在氨基酸序列上具有高度同源性。两种病毒的p10蛋白具有相似的氨基酸组成，并且两者的N端埃德曼降解均受阻。两种病毒的磷蛋白均含有磷酸丝氨酸，但在氨基酸组成、分子量和N端氨基酸序列上彼此不同。因此，数据表明所检测的R - D/W的每种蛋白都与其MPMV同源物不同，并且这两种D型逆转录病毒之间的主要差异存在于病毒磷蛋白中。D型逆转录病毒蛋白的N端氨基酸序列用于搜索D型与其他逆转录病毒氨基酸序列之间的序列同源性。在R - D/W pp20（一种gag蛋白）与劳斯肉瘤病毒env前体多蛋白的一个28个残基的片段之间发现了意外的氨基酸序列同源性。D型主要gag蛋白（p27）和核酸结合蛋白（p14）的N端氨基酸序列与C型逆转录病毒的功能同源蛋白仅显示有限的氨基酸序列同源性。
