Journal
VIROLOGY
Volume 298, Issue 2, Pages 317-326Publisher
ACADEMIC PRESS INC ELSEVIER SCIENCE
DOI: 10.1006/viro.2002.1497
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We have examined the consequences of cleaving the fusion glycoprotein (F) of human respiratory syncytial virus (HRSV) at two distinct furin-recognition sites. Purified anchorless IF is a mixture of unaggregated cone-shaped molecules and rosettes of lollipop-shaped spikes. The unaggregated molecules contain a proportion of uncleaved F0 and an intermediate, FDelta1-109, cleaved only at site I, residues 106-109. Inhibition of cleavage at site 1, by two amino acid changes (R108N/R109N), reduces the proportion of aggregated molecules with a concomitant increase in the amount of unprocessed F0. Inhibition of cleavage at site II, residues 131-136, by deletion of four amino acids (Delta131-134), abrogates aggregation of anchorless F and all molecules are seen as individual cone-shaped rods. In vitro cleavage of anchorless F, or mutant Delta131-134, with trypsin at 4, 20, or 37degreesC, under conditions in which cleavage at site II is complete in all molecules, leads to their aggregation in rosettes of lollipop-shaped spikes. Thus, cleavage at site II is required for the structural changes in anchorless F that lead to changes in shape and to aggregation. The segment between sites I and II, residues 110-136, is not associated with anchorless F in the supernatant of infected cell cultures, indicating that it is released from the processed protein when cleavage at sites I and II is completed. (C) 2002 Elsevier Science (USA).
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