Open reading frame 2 of porcine circovirus type 2 encodes a major capsid protein.
نویسندگان
چکیده
Porcine circovirus 2 (PCV2), a single-stranded DNA virus associated with post-weaning multisystemic wasting syndrome of swine, has two potential open reading frames, ORF1 and ORF2, greater than 600 nucleotides in length. ORF1 is predicted to encode a replication-associated protein (Rep) essential for replication of viral DNA, while ORF2 contains a conserved basic amino acid sequence at the N terminus resembling that of the major structural protein of chicken anaemia virus. Thus far, the structural protein(s) of PCV2 have not been identified. In this study, a viral structural protein of 30 kDa was identified in purified PCV2 particles. ORF2 of PCV2 was cloned into a baculovirus expression vector and the gene product was expressed in insect cells. The expressed ORF2 gene product had a molecular mass of 30 kDa, similar to that detected in purified virus particles. The recombinant ORF2 protein self-assembled to form capsid-like particles when viewed by electron microscopy. Antibodies against the ORF2 protein were detected in samples of sera obtained from pigs as early as 3 weeks after experimental infection with PCV2. These results show that the major structural protein of PCV2 is encoded by ORF2 and has a molecular mass of 30 kDa.
منابع مشابه
Complete Genomic Sequence of a Novel Porcine Circovirus 2 Strain, CC12
The genome sequence of a novel porcine circovirus 2 strain (CC12) is composed of 1,767 nucleotides, with two major open reading frames (ORFs). ORF1 encodes two replication-associated proteins (Rep and Rep') with the unique mutation N186S, and ORF2 encodes a viral capsid protein (Cap) with two rare mutations, R59K and A190T.
متن کاملMapping of the nuclear localization signals in open reading frame 2 protein from porcine circovirus type 1.
Porcine circovirus type 1 (PCV1) contains two major open reading frames encoding the replication-associated proteins and the major structural capsid (Cap) protein. PCV1 Cap has an N-terminus carrying several potential monopartite or bipartite nuclear localization signals (NLS). The contribution of these partially overlapping motifs to nuclear importing was identified by expression of mutated PC...
متن کاملNuclear localization of the ORF2 protein encoded by porcine circovirus type 2.
Infectious porcine circovirus type 2 (PCV2) was generated following transfection of a porcine retina cell line (VIDO R1) with cloned circovirus DNA. Expression of open reading frame 2 (ORF2) was detected at 24 h postinfection and onwards increasingly throughout the infection by Western blot analysis using ORF2 specific polyclonal antibody. Moreover, the ORF2 protein was also detected in purifie...
متن کاملAntibody recognition of porcine circovirus type 2 capsid protein epitopes after vaccination, infection, and disease.
Open reading frame 2 (ORF2) of porcine circovirus type 2 (PCV2) codes for the 233-amino-acid capsid protein (CP). Baculovirus-based vaccines that express only ORF2 are protective against clinical disease following experimental challenge or natural infection. The goal of this study was to identify regions in CP preferentially recognized by sera from experimentally infected and vaccinated pigs an...
متن کاملIdentification of a protein essential for replication of porcine circovirus.
The largest open reading frame of porcine circovirus (ORF 4) encodes a protein of 312 amino acids. The predicted gene product of ORF 4 shows similarities to Rep proteins of other plant circoviruses and geminiviruses. Three motifs have been identified that are characteristic for proteins involved in rolling circle replication and the consensus sequence for a putative dNTP-binding box (GKS) has b...
متن کاملذخیره در منابع من
با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید
برای دانلود متن کامل این مقاله و بیش از 32 میلیون مقاله دیگر ابتدا ثبت نام کنید
ثبت ناماگر عضو سایت هستید لطفا وارد حساب کاربری خود شوید
ورودعنوان ژورنال:
- The Journal of general virology
دوره 81 Pt 9 شماره
صفحات -
تاریخ انتشار 2000