用PCR技术从一武汉病人血清中分离获得1TI DNA片断，把此DNA片断克隆到pMD18一T质粒载体中， 进行全序列测定并用计算机软件对核苷酸、氨基酸序列和ORF2多肽特征进行比较和分析。所分离获得的1TI DNA片断全长1333bD，含1TITV完整的ORF2及部分ORF1序列，核苷酸和氨基酸序列与其它基因型为1a的1TI 分离株具有极高的同源性。ORF2多肽含202个氨基酸， 在N端部分和C端部分具有较高的亲水性和较强的抗原 性． 而中问为一段疏水区域，抗原性较弱。N端结构以Of．螺旋为主，含有典型的酪氨酸激酶磷酸化价点(RARD． WPGY，38—45aa)和三个潜在的蛋白质激酶C的磷酸化位点；C端富含脯氨酸，结构以B转向为主，含有三个连 续的N一十四烷酰化位点，推测ORF2编码的蛋白可能是一种磷酸化蛋白。

A T1 DNA fragment was obtained from W uhan patient serum by PCR，which was cloned into plasmid pMDl8—-T and analyzed by sequencing combined with computer techniques comparing withother isolated strains．The results reveal that this DNA fragment consists of 1 333 base pairs containing whole Trv ORF2 and partial ORFI coding regions， the DNA and deduced amino acid sequence are highly homogenous with those of 1TrV la type．ORF2 peptide consists of 202 amino acids． whose parts of N terminal and C term inal have comparatively high hydrophilic and strongly antigenic characters than middle part．Th e part near N term inal contains a typical tyrosine kinase phosphorylation site(RARDWPGY，38-45aa) and 3 potential protein kinase C phosphorylation sites， the structure in N terminal part is mainly仅helices：while the part near C term inal contains proline rich region and 3 consecutive N-myristoylation sites，the structure in C terminal part is mainly B turns．We infer that the ORF2 protein maybe a phospholated Protein