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G J Cox

Publications and source records attributed to G J Cox.

29 records · Page 2Linked to original sources
PubMed1990

Primary structure of the S peplomer gene of bovine coronavirus and surface expression in insect cells.

The nucleotide sequence of the S peplomer gene of bovine coronavirus (BCV) has been determined. A single open reading frame of 4089 nucleotides encodes a polypeptide of 150K with 20 potential sites for addition of N-linked oligosaccharides. Expression of the cloned BCV S gene by a recombinant of Autographa californica nuclear polyhedrosis virus resulted in production of a 180K glycosylated polypeptide which was transported to the surface of the cell. Comparison of the BCV S gene with the analogous genes of murine hepatitis viruses shows that the BCV S polypeptide contains a unique domain of 138 amino acids not present in murine hepatitis virus strain JHM, but which has a partially homologous counterpart in strain A59. This domain accounts for most of the differences in size of the S gene products of these coronaviruses.

Amino Acid Sequence↗
PubMed1989

Cloning and in vitro expression of the gene for the E3 haemagglutinin glycoprotein of bovine coronavirus.

A cDNA clone representing the gene for the E3 glycoprotein, the haemagglutinin, of bovine coronavirus was isolated from a plasmid cDNA library of the viral genome and sequenced. The gene is located immediately 5' of the E2 glycoprotein gene on the viral genome. Nucleotide sequencing of the E3 gene predicts a polypeptide of 424 amino acids with an Mr of 47K. In vitro translation of mRNA transcribed from the cloned E3 gene yielded a polypeptide of Mr 45K, similar to that predicted from the nucleotide sequence. In the presence of microsomal membranes, the in vitro product was cotranslationally processed to a 62K polypeptide which comigrated on SDS-polyacrylamide gels with the E3 monomer (gp62) obtained from virus-infected cells. Both the 45K and 62K polypeptides were immunoprecipitated with E3-specific monoclonal antibodies, confirming the identity of the gene as that encoding the E3 glycoprotein. Finally, only monoclonal antibodies to the E3 protein inhibited haemagglutination by the virus thus confirming its identity as the haemagglutinin of bovine coronavirus.

Amino Acid Sequence↗
PubMed1988

Oral acanthosis nigricans: report of a case and comparison of oral and cutaneous pathology.

Malignant acanthosis nigricans is usually associated with adenocarcinomas of the digestive tract. The lesions of acanthosis nigricans commonly run a parallel course to the associated malignancy, producing hyperpigmented, roughened plaques on the skin and, sometimes, verruca-like papules on the oral mucosa. The clinical differences between cutaneous and oral acanthosis nigricans are mirrored by the marked differences in the histopathology. Because oral acanthosis nigricans is uncommon, recognizing histologic features may be difficult. The oral lesions have a true acanthosis and epithelial papillary hyperplasia while the cutaneous forms show slight irregular acanthosis that alternates with areas of epidermal atrophy and dermal papillomatosis.

Acanthosis Nigricans↗
PubMed1986

Toxic erythema of palms and soles associated with high-dose mercaptopurine chemotherapy.

We encountered a case of distinctive palmar-plantar erythema with desquamation of the fingers in a patient receiving high-dose mercaptopurine combined with allopurinol. He was receiving 400 mg/d of mercaptopurine with 200 mg/d of allopurinol when a painful, livid erythema involving his hands and feet developed. Over the ensuing 24 hours, desquamation of the distal fingertips was noted. The mercaptopurine was discontinued and the patient was treated with topical fluocinonide ointment under occlusion. Over the next 96 hours, the erythema and pain resolved entirely. To date, this is the eighth case of a painful desquamating erythema of the palms and soles occurring as a complication of chemotherapy. We suggest that high-dose mercaptopurine combined with allopurinol that blocks xanthine oxidase, a necessary enzyme in the catabolism of mercaptopurine, was responsible for our patient's clinical presentation.

Adult↗