Disease relevance of SHFVgp06

• Here, we analyzed the ORF5 and ORF7 genes for a large number of new European type PRRSV isolates in conjunction with existing database sequences [1].
• The major envelope gene (ORF5) of 51 PRRSV field isolates recovered before and after the introduction of the vaccines was amplified, denatured, and reannealed with the HMA reference vaccine strains Ingelvac PRRS MLV and Ingelvac PRRS ATP, respectively [2].
• ORF 5 encodes the primary virion envelope glycoprotein (VP-3P) (25-42 kDa) [3].
• These results indicate that PRRSV GP5 in principle is a major target for neutralizing antibodies, as is found for other arteriviruses, but that in nature 'ORF 5 escape mutants' may develop as easily as in vitro [4].
• To produce the native form of GP5 in mammalian cells, we have cloned the ORF5 gene from PRRSV CNV-1 into the Semliki Forest virus (SFV)-based expression vector, resulting in recombinant pSFV-ORF5 [5].

High impact information on SHFVgp06

• Using monospecific antisera as well as an antivirion serum, and by expression of individual ORFs, the genes for the structural proteins were identified: ORF 7 codes for N, ORF 6 for M, ORF 5 for GL, and ORF 2 for GS [6].
• The gene encoding glycoprotein 5 (ORF5) of 21 porcine reproductive and respiratory syndrome virus (PRRSV) isolates from Spain and two European-type vaccines currently available in that country were analysed using RT-PCR and sequencing [7].
• In order to map the neutralization epitope in the GP(5) protein of the PPV strain, the ORF5 nucleotide sequence of PPV was determined [8].
• Nine point mutations in the ORF5 region resulted from 152 in vitro passages of the V-502 isolate in MARC-145 cells [9].
• Using this method a single neutralization epitope has been shown to be located in the very short (about 30 amino acid long) ectodomain of the primary envelope glycoprotein, VP-3P, encoded by ORF 5 [10].

Chemical compound and disease context of SHFVgp06

• Five groups received MLV vaccine with either bacterial endotoxin-derived adjuvant (ET), mixed open reading frame 5 (ORF5) peptides derived from various PRRSV isolates, porcine interferon alpha (IFNalpha), polyinosinic-polycytidylic acid stabilized with polylysine and carboxymethylcellulose (poly-ICLC), or porcine interleukin-12 (IL-12) [11].

Biological context of SHFVgp06

• A region of the PRRS virus genome containing portions of ORF4 and ORF5 was amplified directly from tissues of infected pigs from birth to 132 days of age [12].
• The ORF5 nucleotide identities within the US genotype tested in this study compared to the US prototype, VR-2332 varied from 83.7 to 85.2%, whereas 83.5-85.5% amino acid identities were found [13].
• ORF5 products of the eight US strains (00CS1, 01NP1, 01UD6, 02CB13, 02KK1, 02PB1, 02SP2 and 02SP3) and the six EU strains (01CB1, 01RB1, 02BR1, 02CB12, 02SB2 and 03RB1) were sequenced for genetic variation analysis [13].
• The variability of the deduced ORF5 amino acid sequences was analysed using statistical process control (SPC), allowing for the objective assessment of variable and conserved regions [14].
• Differentiation of a porcine reproductive and respiratory syndrome virus vaccine strain from North American field strains by restriction fragment length polymorphism analysis of ORF 5 [15].

Anatomical context of SHFVgp06

• The group immunized with only ORF5 peptide/CT did not have significant T-cell recall responses and was not protected from challenge [11].
• In vitro transcription/translation of the ORFs 5 of LDV-P and LDV-v indicated that all three N-glycosylation sites in the ectodomain of LDV-P VP-3P became glycosylated when synthesized in the presence of microsomal membranes, whereas the glycosylation of the ORF 5 proteins of LDV-v and LDV-C was consistent with glycosylation at a single site [16].
• Sublines of Marc-145 and HeLa cells were established by stable transfection with open reading frame (ORF)4 and ORF5 of PRRSV, respectively, and differential gene expressions were studied using microarray chips embedded with 1718 human-expressed sequence tags [17].
• Moreover, ORF 5 protein was localized both in the perinuclear region and the Golgi complex and transported to the cell surface [18].

Associations of SHFVgp06 with chemical compounds

• ORF 5 encoding the primary envelope glycoprotein, VP-3P, of a highly neuropathogenic isolate of lactate dehydrogenase-elevating virus (LDV-v) has been sequenced [16].

Other interactions of SHFVgp06

• ORF 5, which encodes the envelope glycoprotein, was the most polymorphic [total nucleotide diversity (pi) = 0.097 +/- 0.007] and ORF 6, encoding the viral M protein, was the most conserved (pi = 0.038 +/- 0.003) [19].
• The results also indicate that neutralization epitopes for PRRS virus are present on the viral envelope glycoproteins encoded by ORF 4 and ORF 5 [20].

Analytical, diagnostic and therapeutic context of SHFVgp06

• In the present study we identified the presence of three different quasispecies in another original neuropathogenic LDV by sequence analysis of cDNA clones of ORF 5 (encoding the primary envelope glycoprotein VP-3P) obtained from the isolate [21].
• In conclusion, booster immunizations of the mixed ORF5 peptides and co-administration of IL-12 effectively enhanced the CMI response to MLV vaccine [11].
• Subsequent sequencing of the PCR products from ORF5 and phylogenetic analysis revealed the occurrence of both the European and the American-type of porcine reproductive and respiratory syndrome virus in Austria [22].
• Pigs intradermally injected twice with hAdV/ORF5 developed antibody titers to the authentic viral GP(5) as soon as 10 days following challenge with the homologous virulent PRRSV strain, as revealed by Western blot and virus neutralization tests, suggesting the establishment of a specific immune memory [23].
• Indeed, when the expression cassette was turned-on, caspase 3 activity in hAdV/ORF5 infected cells was enhanced and DNA fragmentation could be detected by TUNEL assays [23].

References