The influenza virus neuraminidase (NA), a type II transmembrane glycoprotein, is expressed at the surface of infected cells and is a major structural component of the virion. The kinetics of biosynthesis of NA, including modification of N-linked sugar chains, association with GRP78-BiP, oligomerization, and transport to the cell surface, were examined in A/WSN/33 influenza-infected BHK cells. Prior to gaining endoglycosidase H (endo H) resistance, NA was found to transiently associate with GRP78-BiP (t21 ≈ 5 min). The protein was synthesized as a monomer and within 10 min a significant fraction of it was chased into dimers and tetramers with a t 1 2 ≈ 15 to 20 min before endo H resistance was acquired suggesting that oligomerization took place in the endoplasmic reticulum. WSN NA remained completely endo H sensitive up to 15 min after synthesis, acquired partial resistance to endo H between 15 and 30 min (t 1 2 ≈ 25 min) after synthesis and exhibited heterogeneity in endo H-resistant forms. NA was first detected at the cell surface 30 min after synthesis, increased to a maximum at 1 hr, after which it decreased, presumably due to incorporation into virions. The results on the biosynthesis of NA, a type II protein for which the three-dimensional structure is known, will be useful in structure/function and virion assembly studies.
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