Nectin1 Recombinant Protein (BV)
- Known as:
- Nectin1 Recombinant Protein (BV)
- Catalog number:
- HA266050
- Product Quantity:
- 50
- Category:
- -
- Supplier:
- Viagen
- Gene target:
- Nectin1 Recombinant Protein ()
Related genes to: Nectin1 Recombinant Protein (BV)
- Gene:
- NECTIN1 NIH gene
- Name:
- nectin cell adhesion molecule 1
- Previous symbol:
- HVEC, ED4, PVRL1
- Synonyms:
- PRR, PRR1, PVRR1, SK-12, HIgR, CLPED1, CD111, OFC7
- Chromosome:
- 11q23.3
- Locus Type:
- gene with protein product
- Date approved:
- 1999-11-15
- Date modifiied:
- 2016-02-12
Related products to: Nectin1 Recombinant Protein (BV)
Related articles to: Nectin1 Recombinant Protein (BV)
- Herpes simplex virus 1 (HSV‑1) establishes infection through coordinated interactions of multiple viral glycoproteins with host cell receptors. Interactions between the viral glycoprotein D (gD) and the immunomodulatory cellular receptor HVEM (herpesvirus entry mediator) critically influence HSV‑1 latency and reactivation by regulating both receptor engagement and immunomodulatory signaling in the corneal epithelium, immune cells, and neurons. The underlying mechanisms of these phenotypes remain poorly understood because no tools selectively block their interaction. To dissect the contributions of individual amino acids (aa) to HVEM binding, we co‑immunoprecipitated wild‑type (WT) and mutant (Q27P and Q27A‑L28A‑T29A) forms of gD that disrupt gD binding to HVEM. We found that gD aa Q27-T29 were critical for HVEM binding, with the triple mutant showing greater disruption of HVEM binding than the Q27P single mutation, as assessed by co-immunoprecipitation and immunostaining. To map gD binding to HVEM and assess functional relevance, we constructed two recombinant viruses: a single-amino-acid (aa) gD mutation (v27 virus) and a triple-aa mutation in gD (v27-29 virus). Replication of both mutant viruses was comparable to that of the WT virus in four mammalian cell lines, except in Neuro2a cells. However, using confocal microscopy, HVEM protein expression was reduced in v27-29-infected Neuro2a cells, with no gD colocalization observed. Although Neuro2a cells infected with the single gD v27 mutant also showed less HVEM-gD colocalization than Neuro2a cells infected with WT virus, gD protein levels were not affected. RT‑PCR analysis of Neuro2a cells infected with single and triple gD mutants showed significantly less expression of viral glycoproteins (gB, gC, gD), host receptors (HVEM, nectin‑1, 3‑O‑sulfated heparan sulfate), and HVEM ligands (BTLA, LIGHT, Ltα, CD160), with the most pronounced effects observed for the triple v27‑29 mutant virus. Together, these results show that aa Q27-T29, rather than aa Q27 alone, are essential to completely block gD binding to HVEM and, consequently, affect overall receptor homeostasis. - Source: PubMed
Publication date: 2026/09/08
Arya DeepakTormanen KatiOh Jay JWang ShaohuiGhiasi Homayon - Orofacial cleft is a congenital anomaly influenced by genetic and environmental factors. encodes an adhesion protein critical for the adherens junctions and has been associated with orofacial clefts. This study aimed to investigate the contribution of to the etiology of NSCL/P in a population from Patagonia, Argentina, a region with a high prevalence of orofacial clefts. - Source: PubMed
Publication date: 2026/08/13
Meneguci Moreira Franco Ana LuizaAntunes DeborahProença da Fonseca Ana CarolinaRodrigues Moreira Gomes Ana ClaraRamos Guimarães Ana CarolinaOrioli Ieda MariaMartinez de Carvalho Flavia - Herpes B virus (BV; ) is a zoonotic alphaherpesvirus endemic in macaques that can cause severe, often fatal encephalomyelitis in humans. However, genomic data from wild macaque populations remain limited. Here, we report the isolation and genomic characterization of a BV strain from a wild long-tailed macaque () in Thailand and assess its zoonotic potential. Among 138 macaques screened across six populations, BV shedding was detected in a single oral swab (0.72%). The virus (BV/Thailand/Ranong_TPK5/2024) was successfully isolated and propagated in Vero and LLC-MK2 cells, with higher replication efficiency observed in Vero cells. The TPK5 isolate exhibited a high infectious titre (8 × 10⁷ PFU/mL), and transmission electron microscopy confirmed typical herpesvirus morphology. Whole-genome sequencing achieved deep coverage (∼20,974×) and revealed 98.4% identity to a reference strain (E90-136) from captive long-tailed macaques. Phylogenetic analyses of 12 envelope glycoproteins demonstrated host-associated clustering, with the TPK5 isolate grouping within the long-tailed macaque lineage. Key entry glycoproteins (gB, gD, gH, and gL) were highly conserved among macaques but diverged from human herpes simplex viruses. In contrast, host receptors nectin-1 and nectin-2 were highly conserved between macaques and humans (≥95% identity), suggesting preserved receptor compatibility. Despite the low prevalence of shedding, the isolation of an infectious BV strain from an asymptomatic macaque highlights an ongoing zoonotic risk. Conservation of viral entry mechanisms and host receptors supports the potential for cross-species transmission in high human-macaque interface settings. - Source: PubMed
Publication date: 2026/07/20
Paungpin WeenaChaiwattanarungruengpaisan SomjitThongdee MetaweeSariya LadawanSapkanarak KrittigaKemthong TaratornDangsagul WorawatSuwanpakdee SarinWiriyarat WitthawatMalaivijitnond Suchinda - The alphaherpesvirus (PRV), which causes Aujeszky's disease (AD), primarily infects swine but has zoonotic potential and can infect multiple species, including humans. Upon infection, interferons (IFNs) trigger the expression of hundreds of interferon-stimulated genes (ISGs), thereby establishing a robust cellular antiviral state. However, ISGs exhibiting anti-alphaherpesvirus activity have not yet been fully characterized. Here, we perform an unbiased screen of 268 ISGs and identify Nectin4, also known as PVRL4, as a potent antiviral ISG against alphaherpesvirus, including herpes simplex virus (HSV). Mechanistically, Nectin4 inhibits viral internalization into host cells, in which the IgV domain plays a critical role. Specifically, Nectin4 interacts with the viral gD protein through this domain, thereby inhibiting the interaction between gD and viral receptor, Nectin1, and blocking gD-mediated viral entry. Together, our data identify a previously unrecognized function of Nectin4 in host anti-alphaherpesvirus immunity and highlight a novel cellular barrier that restricts alphaherpesvirus infection. - Source: PubMed
Publication date: 2026/07/20
Wang YiBo ZongyiZhao SenhongFazlani Tanveer AliYang FayuFeng ZhengshanCao TianxingZhang ZhonghuiXue WenchaoChen ShuaiQiao YupanZhu ZixiangCheng GenhongWang YipingZheng HaixueZhang Shilei - Glioblastoma (GBM) remains one of the most aggressive and lethal malignancies, with clinical outcomes under the standard-of-care Stupp protocol remaining suboptimal. While oncolytic virus (OV) therapy has emerged as a mechanistically distinct and promising approach, its clinical success is frequently hindered by profound intratumoral heterogeneity and emerging resistance. This critical review proposes that the efficacy of virotherapy may be meaningfully enhanced by integrating circadian biology into treatment schedules; a paradigm termed "Oncolytic Chronovirotherapy." Recent evidence demonstrates that the infection cycle of neurotropic viruses, which serve as the scaffold for many OVs, is not a static process but is inherently regulated by the host's circadian clock. Fundamental studies reveal that the expression of essential viral entry receptors, such as Nectin-1 (for HSV-1) and p75NTR, exhibits robust circadian oscillations directly coordinated by the core molecular clock, specifically the BMAL1/CLOCK complex. Furthermore, the tumor immune microenvironment and cellular vulnerability to adjuvant chemotherapy (temozolomide) show synchronized peaks of activity, typically concentrated during the morning window, which often coincides with the nadir of DNA repair enzymes like MGMT. We argue that synchronizing OV administration with these windows of maximal receptor density and robust immune surveillance may maximize tumor lysis and facilitate the conversion of "cold" tumors into "hot," immune-responsive environments. The utilization of personalized circadian biomarkers and mathematical modeling to guide therapy delivery will be essential for the next generation of precision neuro-oncology. - Source: PubMed
Publication date: 2026/07/06
Guterres Alexandro