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Polypeptides of murine and avian pneumoviruses

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Ling, Roger (1988) Polypeptides of murine and avian pneumoviruses. PhD thesis, University of Warwick.

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Official URL: http://webcat.warwick.ac.uk/record=b1453393~S1

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Abstract

The work described in this thesis identifies some
properties of the major polypeptides of pneumonia virus of
mice (PVM) and of turkey rhinotracheitis (TRT) virus. The
PVM glycoproteins have been studied in particular detail
while the results obtained with TRT virus provide a
preliminary description of the polypeptides of this virus.
Twelve major PVM specific polypeptides designated L, G1,
G2, F1, N, 39K, 35K, M, 20K, 19K, 16K and 12K were
identified. In addition PVM specific polypeptides
designated 25K, 24K, 23K, 18K and 17K were sometimes
detected. Monoclonal antibodies directed against the G1/G2,
39K and M polypeptides were produced.
The a~ility of a monoclonal antibody to precipitate
G1 and G2 suggested that these two glycosylated proteins
were related and this was confirmed by tryptic peptide
mapping. G2 was shown to be derived from G1 in pulse chase
experiments and a similar relationship between two higher
mobility polypeptides synthesized in the presence of
tunicamycin was observed. The G protein may have a
precursor since G1 did not appear immediately following a
pulse labelling. The precursor could not however be
identified. An additional minor glycosylated polypeptide of
42K was found to be related to the G protein.
The F1 protein appeared to be poorly glycosylated and
a difference in mobility of the polypeptide synthesized in
the presence of tunicamycin did not appear to be directly
due to a lack of N-linked oligosaccharides. The polypeptide
migrated more slowly under non-reducing conditions but no
evidence of a small disulphide bonded polypeptide was found
in contrast to the situation with other paramyxoviruses.
This polypeptide appeared to be the major PVM protein
expressed on the cell surface and was associated with G1
and G2 as the major protein in a particulate fraction of
the infected cell supernatant.
Tentative relationships were suggested between the
39K, 35K and 25K polypeptides, the M and 24K polypeptides
and the 20K and 19K polypeptides. This together with the
observation that the 12K polypeptide was not a primary gene
product suggested that there may be about 11 PVM
polypeptides. The N or 39K and the 20K or 19K polypeptides
were observed to be phosphorylated.
Twelve possible TRT virus specific polypeptides of
150K, 129K, 95K, 83K, 57K, 45K, 38K, 35K, 3DK, 23K, 19K and
15K were identified. The 150K, 95K, 83K, 57K, 45K and 15K
polypeptides were glycosylated with the latter three
polypeptides showing a similar relationship to the F1,2, F1
and F2 polypeptides of paramyxoviruses. A broad
glycosylated band designated the 31K polypeptide was
identified that was similar to a smeared band observed on
prolonged exposure of immunoprecipitates of PVM
polypeptides labelled with [3H]-glucosamine. The 35K and
19K polypeptides were observed to be phosphorylated.
PVM may be more closely related to RS virus than TRT
virus since anti-PVM serum irnmunoprecipitated the RS virus
N polypeptide but not any TRT virus polypeptides. The PVM
39K polypeptide and the RS virus P protein were recognised
by a monoclonal antibody providing further evidence of a
relationship between PVM and RS virus.

Item Type: Thesis (PhD)
Subjects: Q Science > QH Natural history > QH301 Biology
Q Science > QR Microbiology > QR355 Virology
Library of Congress Subject Headings (LCSH): Polypeptides , Viral diseases -- Research, Viral pneumonia -- Research, Pneumonia -- Research, Birds
Official Date: May 1988
Dates:
DateEvent
May 1988Submitted
Institution: University of Warwick
Theses Department: Department of Biological Sciences
Thesis Type: PhD
Publication Status: Unpublished
Supervisor(s)/Advisor: Pringle, Craig R.
Sponsors: Science and Engineering Research Council (Great Britain) (SERC)
Extent: 2 volumes
Language: eng

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