Disease relevance of US6

• In this article, we demonstrate that the varicellovirus protein UL49.5, in contrast to ICP47 and US6, strongly impairs the activity of the mouse transporter and mediates degradation of mouse TAP1 and TAP2 [1].
• First, soluble mNectin1delta failed to physically interact with HSV glycoprotein D (gD) at a detectable level, although it interacted physically with virions [2].
• The murine homolog of human Nectin1delta serves as a species nonspecific mediator for entry of human and animal alpha herpesviruses in a pathway independent of a detectable binding to gD [2].
• A single oral exposure in utero to plasmid DNA encoding a truncated form of glycoprotein D of bovine herpesvirus-1 induced detectable immune responses in 80% (12 of 15) of newborn lambs [3].
• Identification of a site on herpes simplex virus type 1 glycoprotein D that is essential for infectivity [4].

High impact information on US6

• Alpha-herpesvirus glycoprotein D interaction with sensory neurons triggers formation of varicosities that serve as virus exit sites [5].
• The chimeric tgD-CD154 was expressed in vitro in COS-7 cells and reacted with both glycoprotein D- and CD154-specific Abs [6].
• The entry of herpes simplex virus (HSV) into cells requires the interaction of viral glycoprotein D (gD) with a cellular gD receptor to trigger the fusion of viral and cellular membranes [7].
• Nectin-1, a member of the immunoglobulin superfamily, can serve as a gD receptor for HSV types 1 and 2 (HSV-1 and HSV-2, respectively) as well as for the animal herpesviruses porcine pseudorabies virus (PRV) and bovine herpesvirus 1 (BHV-1) [7].
• Transcriptional analysis of Marek's disease virus glycoprotein D, I, and E genes: gD expression is undetectable in cell culture [8].

Chemical compound and disease context of US6

• These data are consistent with previous reports by others that cellular expression of the BHV-1 gIV homologs, herpes simplex virus glycoprotein D, and pseudorabies virus glycoprotein gp50 provide partial resistance against infection with these viruses [9].
• There is evidence that it recognizes a specific receptor after initial attachment of virions to cell surface heparan sulfate and also that gD-1, gD-2, and gp50 (the pseudorabies virus gD homolog) bind to the same receptor [4].
• In this study, we have investigated the use of RN-205 (immunomodulator containing a membrane rich in lipopolysaccharide from gram-negative bacteria) as an adjuvant and analyzed the humoral and cellular specific immune responses elicited by DNA vaccines based on the bovine herpesvirus-1 (BHV-1) glycoprotein D (gD) [10].

Biological context of US6

• Therefore, the MDV gD gene expression is down-regulated at the transcription level in MDV-infected cell culture, which may be related to the cell-associated nature of MDV in fibroblast cells [8].
• Marker rescue experiments revealed that a single point mutation in the first position of codon 450 of the glycoprotein H open reading frame, resulting in a glycine-to-tryptophan exchange, enabled complementation of the gD function for cell-to-cell spread [11].
• Working on the assumption that such a site may overlap with a functional region of gD, we showed previously that combining two or more amino acid substitutions within site I prevents gD-1 from functioning and is therefore lethal [4].
• In contrast, integration of the gD gene into the genomes of gD-infBHV-1 and ctcs+BHV-1/80-221 resulted in recombinants with accelerated penetration in comparison to wild-type virions [11].
• In addition, the loss of VP22 tyrosine phosphorylation correlated with reduced incorporation of VP22 compared to that of envelope glycoprotein D in the mutant viruses but not with the amount of VP22 produced during virus infection [12].

Anatomical context of US6

• We also demonstrated that the cell compartment in which plasmid-encoded gD was expressed caused a deviation in the serum immunoglobulin (Ig) isotype profile as well as the predominant cytokines secreted from the draining lymph node [13].
• To test this hypothesis, we constructed a BHV1.1 gD-expressing cell line (MDBKgD) and assessed its resistance to the homologous BHV1.1 and two closely related viruses, BHV1.2 and BHV5 [14].
• As an approach to induce mucosal immunity against bovine herpesvirus-1, cows were immunized intravaginally with suppositories containing plasmid coding for glycoprotein D. Serum IgG, as well as IgA both in the serum and in the nasal fluids, were detected, which supports the contention of a common mucosal immune system [15].
• Alphaherpesviral glycoprotein D (gD) is a critical component of the cell membrane penetration system [14].
• We investigated the antigen-specific mucosal and systemic immune responses of newborn lambs following enteric immunization, targeting jejunal Peyer's patches with a human adenovirus vector that expressed the glycoprotein D (gD) of bovine herpesvirus-1 [16].

Associations of US6 with chemical compounds

• Characterization of caprine herpesvirus 1 glycoprotein D gene and its translation product [17].
• Moreover, six cysteine residues are conserved by CpHV-1 gD and the other studied alphaherpesviruses [17].

Other interactions of US6

• An inactivated glycoprotein E-negative vaccine and an experimental glycoprotein D-subunit vaccine against bovine herpesvirus 1 (V1) were examined for their effectiveness in a randomized, double-bline, placebo-controlled field trial comprising 130 dairy farms [18].

Analytical, diagnostic and therapeutic context of US6

• From essential to beneficial: glycoprotein D loses importance for replication of bovine herpesvirus 1 in cell culture [11].
• Using biosensor analysis, we measured the affinity of binding of gD from HSV strains KOS and rid1 to two forms of HveC [19].
• Use of epitope mapping to identify a PCR template for protein amplification and detection by enzyme-linked immunosorbent assay of bovine herpesvirus type 1 glycoprotein D [20].
• A 50 kDa polypeptide was identified in recombinant PAV-3-infected cell lysates by immunoprecipitation assays using gD-specific monoclonal antibodies [21].
• The MAbs 3402 and R54 reacted with the expressed fragments on Western blots that located the epitopes between the amino acids 52-126 and 165-216, respectively, of gD [22].

References