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J. gen. Virol. (1981), 55, 155-164. Printed in Great Britain
Key words: 1B V polypeptides/IB V strains/glycoproteins/phosphoproteins
155
Polypeptides of Infectious Bronchitis Virus. I. Polypeptides of the Virion
By B. LOMNICZI*t AND J. MORSER
Department of Biological Sciences, University of Warwick, Coventry CV4 7AL, U.K.
(Accepted 10 February 1981)
SUMMARY
Infectious bronchitis virus (IBV), strain Beaudette, grown in cultured cells con-
tained five structural proteins with apparent mol. wt. of 170000 (p170), 94000
(gp94), 50000 (pp50) 30000 (gp30) and 26000 (p26). Both gp94 and gp30 are
glycopeptides since they were labelled with [3H]glucosamine. The only phosphoryl-
ated polypeptide was pp50, and both it and gp94 were occasionally resolved into two
bands. Two other polypeptides with mol. wt. of 28 000 (p28) and 14 000 (p 14) were
sometimes associated with the virus. In egg-grown virus two additional proteins were
found with mol. wt. of 110000 (p110) and 75 000 (gp75). The cell protein, actin, was
also found in highly purified IBV virions. Different serotypes of either tissue
culture-grown or egg-grown virus showed one of the two distinct polypeptide
patterns of IBV described by Nagy & Lomniczi (1979) and Collins & Alexander
(1980a, b). Strain Beaudette gave a pattern characteristic of the M type, while strain
Connecticut gave a pattern characteristic of the C type. The polypeptides present in
Connecticut virus were p170, gp98, pp50, gp28 and p26. Thus, the differences
between the two patterns involve the mobility of both the large (gp94/gp98) and
small (gp30/gp28) glycopeptides.
INTRODUCTION
Coronaviruses form a distinct family of enveloped viruses with large single-stranded RNA
genomes of positive polarity (for review, see Robb & Bond, 1979). In the last few years the
molecular biology of coronaviruses has been extensively studied, and from studies on the
protein structure of porcine (Garwes & Pocock, 1975; Pocock & Garwes, 1977), murine
(Sturman, 1977, Sturman & Holmes, 1977; Wege et al., 1979; Bond et aL, 1979) and human
coronaviruses (Hierholzer, 1976; Macnaughton, 1980) a consistent pattern for coronavirus
proteinS has begun to emerge. There is an unglycosylated nucleoprotein (mol. wt. 50000 to
60000) in the inner part of the virion, one or two smaller polypeptides (mol. wt. 20000 to
30000) in the envelope and two or three large (mol. wt. 60000 to 120000) polypeptides, most
of which are glycosylated, plus an even larger glycoprotein (mol. wt. 160000 to 200000)
associated with the spikes.
In the case of the avian coronavirus, infectious bronchitis virus (IBV), the prototype of the
family, the picture is less clear (Bingham, 1975; Alexander & Collins, 1977; Macnaughton &
Madge, 1977; Macnaughton et al., 1977). In these studies no very large tool. wt. > 150000 or
small mol. wt. < 30000 major proteins were reported and a small glycoprotein, equivalent to
the one in mammalian coronaviruses, was not found. Furthermore, no notable differences
were observed when various strains were compared (Macnaughton & Madge, 1977).
Recently, however, the protein pattern of 12 IBV strains belonging to seven known
serotypes were compared and two distinct polypeptide patterns were recognized (Nagy &
tPresent address: Veterinary Medical Research Institute of the Hungarian Academy of Sciences, 1581-
Budapest, P.O. Box 18, Hungary.
0022-1317/81/0000-4496 $02.00 © 1981 SGM