Purnell W. Choppin

TL;DR: The results indicate that the small glycoprotein of paramyxoviruses is biologically active and is involved in virus-induced hemolysis, cell fusion, and the initiation of infection, and provides a biochemical basis for previously observed host-dependent variation in infectivity, and in hemolyzing and cell-fusion induced by paramyxviruses.

TL;DR: The increase in infectivity caused by proteolytic cleavage of the HA polypeptide provides a biochemical explanation for the previously observed enhancement of plaquing efficiency of influenza viruses by the inclusion of pancreation or trypsin in the agar overlay.

TL;DR: Evidence for a Host-Cell Nuclear Requirement for primary Transcription for Primary Transcription is found and evidence for overlapping Coding Regions using Diff erent Reading Frames in Viruses is found.

TL;DR: The finding that with three different paramyxoviruses the biologically active virions possess F1 and F2 polypeptides suggests that this is a general feature of paramyxOViruses, and that the activation of infectivity, cell fusion, and hemolysis is due to a conformational change in the F protein resulting from proteolytic cleavage to form an active complex of two disulfide-linked polypePTide chains.

TL;DR: The results suggest that the oligopeptides competitively interfere with the N-terminal region of the F 1 or HA 2 polypeptides of paramyxoviruses or myxoviruse, respectively, providing a possible new approach to chemical inhibition of viral replication.