Titlebook: Coronaviruses and Arteriviruses; Luis Enjuanes,Stuart G. Siddell,Willy Spaan Book 1998 The Editor(s) (if applicable) and The Author(s), un

Intercept

Characteristics of Remote Sensingng of proteinase, polymerase and helicase proteins from the polyprotein. We have used . expressed recombinant 3CLpro (r3CLpro) to define cleavage sites in carboxy-terminal region of the ORF 1a polyprotein. Polypeptides containing one or more putative 3CLpro cleavage site were translated . from subcl

可转变

The Politics of Love and Struggle,e overexpressed 3CLpro in . as a fusion protein with maltose binding protein (MBP). The MBP-3CLpro fusion protein was purified from contaminating . proteins by amylose column chromatography, and r3CLpro was cleaved from the fusion protein by factor Xa. Recombinant 3CLpro (r3CLpro) was able to cleave

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anaerobic

Boycott

Virus-Receptor Interactions and Interspecies Transfer of a Mouse Hepatitis Virushe MHV receptor, MHVR, a biliary glycoprotein (Bgp1.). Under treatment conditions that completely ablated the replication of the parental MHV strains, CC1 antireceptor antibodies did not block MHV-H2 replication. Following expression of MHVR in normally nonpermissive ST and CRFK cells, infection wit

过于平凡

Human Biliary Glycoproteins Function as Receptors for Interspecies Transfer of Mouse Hepatitis Virusevels of carcinoembryonic antigen (CEA). These data suggested that MHV-H2 may utilize the human Bgp homologue as a receptor for entry into HepG2 cells. To further study MHV-H2 receptor utilization in human cell lines, blockade experiments were performed with a panel of different monoclonal or polycl

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北极熊

Porcine Reproductive and Respiratory Syndrome Virus Infection of Alveolar Macrophages can be Blocked, PBMC and three porcine cell lines (SK, ST and PK-15) as revealed by flow cytometry. This membrane reactivity correlates well with the susceptibility of these cells to a PRRSV infection. Taken together, these data suggest that M Ab 41D3 and 41D5 recognize a potential cellular receptor for PRRSV on