Takeuchi K, Shaughnessy M A, Lamb R A
Department of Biochemistry, Molecular Biology, and Cell Biology, Northwestern University, Evanston, Illinois 60208-3500.
Virology. 1994 Aug 1;202(2):1007-11. doi: 10.1006/viro.1994.1428.
The equine-1 influenza virus A/Cornell/74 (H7N7) hemagglutinin (HA) is cleaved to HA1 and HA2 in the trans Golgi network (TGN) of infected cells. The avian influenza virus A/chicken/Germany/34 (fowl plague virus Rostock) H7 HA is also cleaved to HA1 and HA2 intracellularly in the TGN. To maintain the fowl plague virus Rostock HA in its native form during transport through the TGN, a functioning M2 ion channel activity is required, otherwise the HA undergoes its transition to the low-pH form (Sugrue et al., 1990, EMBO J. 9, 3469-3476). Studies were initiated to investigate if the equine H7 HA has intracellular requirements different from those of the fowl plague virus Rostock HA. We report here that the pH of transition to the low-pH form of the equine-1 HA is approximately pH 5.3 and that the M2 protein ion channel blocker, amantadine, does not have a discernable effect on the native conformation of equine-1 HA during transport through the TGN. Moreover, the equine-1 HA expressed from cDNA does not require coexpression of a functional M2 protein to maintain HA in its native conformation.
马源甲型流感病毒A/康奈尔/74（H7N7）血凝素（HA）在受感染细胞的反式高尔基体网络（TGN）中裂解为HA1和HA2。禽流感病毒A/鸡/德国/34（禽瘟病毒罗斯托克株）H7 HA在TGN内也在细胞内裂解为HA1和HA2。为了在通过TGN运输过程中使禽瘟病毒罗斯托克株HA保持其天然形式，需要有功能的M2离子通道活性，否则HA会转变为低pH形式（Sugrue等人，1990年，《欧洲分子生物学组织杂志》9，3469 - 3476）。启动了研究以调查马源H7 HA是否具有与禽瘟病毒罗斯托克株HA不同的细胞内需求。我们在此报告，马源-1 HA转变为低pH形式的pH约为5.3，并且M2蛋白离子通道阻滞剂金刚烷胺在通过TGN运输过程中对马源-1 HA的天然构象没有明显影响。此外，从cDNA表达的马源-1 HA不需要共表达功能性M2蛋白来维持HA的天然构象。
