本试验利用杆状病毒载体成功地表达狂犬病病毒糖（G）蛋白。从转染重组了日本动物用狂犬病病毒疫苗株RCHL株G蛋白基因的转移载体和野生型杆状病毒DNA的Sf-9细胞中，分离出2个重组杆状病毒克隆。应用印渍法和荧光抗体法（IFA）从重组杆状病毒感染的Sf-9细胞检出了狂犬病毒G蛋白。Sf-9细胞表达的G蛋白与狂犬病毒RCHL株感染NA细胞的G蛋白的分子量一致。35个抗RCHL株G蛋白的单克隆抗体均与重组杆状病毒感染的Sf-9细胞反应，表明表达的G蛋白的抗原性没有发生变异。表达的G蛋白主要分布在Sf-9细胞的膜表面，形成类似环状的荧光，这种荧光与RCHL株感染的NA细胞的荧光相同。

从广西南宁、百色、柳州市采集了犬脑组织268份，从南宁市、博白县捕获蝙蝠320只，以及从南宁市郊捕获野鼠65只。应用RT-PCR技术对犬脑、蝙蝠和野鼠脑组织进行狂犬病病毒检测，并将阳性材料进行小白鼠脑内接种试验。检测结果表明，犬脑的狂犬病病毒阳性率为1.12%，蝙蝠阳性率为0.94%，野鼠阳性率为3.1%。本调查证明了广西除犬之外，野鼠和蝙蝠等野生动物也携带有狂犬病病毒。

The cDNA encoding the VP6 gene of avian rotavirus PO-13 strain was inserted into the bacterial expression vector pET-3a. Upon isopropyl-1-thio-13-D-galactoside induction, the E. coti BL21 (DE3) harboring the vector containing cDNA of the VP6 gene produced an approximately 45-kDa polypeptide, which reacted with rabbit serum against PO-13 strain in Western blotting. To study the antigenic sites on VP6, various deletion mutants were constructed, expressed in E. coli and the reactivity with antigenic site I- and Iispecific MAbs analyzed by Western blotting. Site I, which is shared with all group A mammalian and avian rotaviruses except for chicken rotavirus, was found to be located at amino acid positions 45 to 65, and site II, which probably contributes to an authentic group A antigen common to both mammalian and avian rotaviruses, at amino acid positions 134 to 142.

We have established a hybridoma producing monoclonal antibody (MAb) against a linear epitope of glycoprotein (G protein) of the RC-HL strain of rabies virus. This MAbl5-13 showed almost the same neutralizing activity to all of five rabies fixed strains, including RC-HL, and reacted to the denatured G protein in western blot analysis. To characterize and map this linear epitope, an antigenic variant NR15-13 was selected from RC-HL strain in the presence of neutralizing MAbl5-13. The variant reacted with MAbl5-13 in an immunofluorescent antibody test but was not neutralized by the antibody and the antibody did not bind to the variant G protein in a Western blot analysis. The variant NR15-13 had an amino acid substitution at position 251 of the G protein, where tryptophan of the parental RC-HL strain was replaced by arginine. Site-directed mutagenesis analysis using the expression system in simian COS7 cells revealed that a single amino acid substitution at 251-tryptophan by arginine on the G protein of the parental RC-HL strain abolished the antigenicity of the epitope for MAbl5-13 in western blot analysis, and the replacement of 251-arginine by tryptophan recovered the activity. These results strongly suggest that tryptophan at position 251 on the G protein is essential for construction of the linear epitope against MAbl5-13.