SUMMARYAvian rotaviruses were isolated from feral pigeon faeces treated with trypsin using roller tube cultures of mammalian cells. Two pigeon strains, designated as strains PO-8 and PO-13, produced a marked cytopathic effect (CPE), small intracytoplasmic inclusion bodies and high titres of infectious particles in infected MA-104 and MDBK cell lines without cell adaptation and roller drum apparatus. The pigeon rotaviruses shared a common group specific antigen with the Lincoln strain of bovine rotavirus by indirect immunofluorescence, but differed from both the Lincoln strain and the Wa strain of human rotavirus in neutralization tests.
By immunoblot analyses of normal human epidermal extracts, the 230 kDa bullous pemphigoid antigen (BP230) is recognized by most bullous pemphigoid sera. By polymerase chain reaction using keratinocyte cDNA library as a template, we successfully amplified 3 cDNAs of about 3 kb, which covered whole human BP230 molecule. By inserting the cDNAs into bacterial expression vector pGEX, we prepared 3 different recombinant glutathione-S-transferase-fusion proteins, which roughly presented N-terminal domain, central rod domain and C-terminal domain of BP230. By immunoblotting using these 3 recombinant proteins, we demonstrated that the majority of bullous pemphigoid sera reacted clearly with multiple recombinant proteins of BP230, most frequently with C-terminal domain. We also examined sera of pemphigus vulgaris, pemphigus foliaceus and herpetiform pemphigus that showed BP230-like protein band by immunoblotting of epidermal extracts, as well as paraneoplastic pemphigus, for reactivity with the 3 recombinant proteins. In the study, we found that only very few of these non-bullous pemphigoid sera reacted with some of the recombinant proteins. These results indicate that the BP230 is specifically reacted by bullous pemphigoid sera, and that the immunoblotting using the BP230 recombinant proteins should be a useful tool for the diagnosis of bullous pemphigoid.
Monoclonal antibodies (MAbs) were prepared to analyze antigens on the major inner capsid protein, VP6 of avian group A rotavirus. Based on the results of a competitive binding assay using 15 MAbs directed against VP6 of the PO-13 rotavirus strain, isolated from a pigeon in Japan, it was found that VP6 of avian rotavirus possesses at least four spatially distinct antigenic sites. Two antigenic sites (I and II) were topologically distinct from the other two (III and IV), which were in close proximity. From the reaction of MAbs in indirect immunofluorescent antibody tests to a series of known rotaviruses, epitopes representing common antigens of all group A rotavirus including avian rotavirus were localized in sites II and III. One epitope in site IV appeared to have a subgroup antigenic specificity that reacted only with rotaviruses belonging to subgroup I. Interestingly, avian rotaviruses isolated from turkeys and chickens in Northern Ireland also reacted only with these subgroup I specific MAbs, but not with subgroup II specific MAb. This indicates that avian rotavirus has subgroup I specific antigen, which is antigenically similar to that of other mammalian rotavirus strains.
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