Ask about this productRelated genes to: PVRL1 antibody
- 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: PVRL1 antibody
Related articles to: PVRL1 antibody
- Pseudorabies virus (PRV), an α‑herpesvirus, has recently been recognized as a potentially significant zoonotic pathogen, causing severe encephalitis and endophthalmitis in humans with high mortality and disability rates. Despite its growing public‑health threat, no effective therapeutics are available for human PRV infection. Here, we isolated a broadly neutralizing monoclonal antibody, designated 6F7, which targets the PRV glycoprotein D (gD) and neutralizes all tested PRV lineages. Mechanistic studies reveal that 6F7 does not impede viral attachment or internalization; instead, it specifically blocks the fusion of the viral envelope with cellular membranes, thereby preventing viral replication. Moreover, the antibody also potently suppresses cell‑to‑cell spread of PRV. We demonstrate that the interaction between gD and the PRV receptor Nectin‑1 is blocked by 6F7. Last, a humanized version of 6F7 confers complete protection in mice challenged with a lethal PRV variant and blocks the establishment of latency at a dose of 15 mg/kg per mouse. Overall, the humanized broadly neutralizing antibody represents a promising therapeutic candidate for human PRV infection. - Source: PubMed
Publication date: 2026/05/19
Sun YueLiu JianboXu Shi-JiaWang Meng-XinZhang HongliangZhang YanheTian Zhi-JunPeng Jin-MeiYin XinAn Tong-QingCai Xue-HuiTang Yan-Dong - Advanced Prostate Cancer (PCa) management suffers from therapeutic resistance due to naturally transient or AR-dependent expression of clinically actionable surface targets. We aimed to identify the most promising clinically relevant PCa targets using RNA and protein expression levels across the PCa continuum-hormone-sensitive, castration-resistant, neuroendocrine, and "double-negative" prostate cancer (DNPC). - Source: PubMed
Publication date: 2026/04/29
Sharma ShivangMundhara NikitaTekoglu EmirhanAmaral AdriannaGu PanLuo JunXie SeanKonchou Morelle MeeganePepra-Ameyaw PatienceDe Marzo Angelo MBrennen W NathanielBaraban Ezra GLotan Tamara LLack Nathan AShenderov Eugene - Puncta adherentia junctions (PAJs) have been observed at glutamatergic excitatory synapses on glutamatergic excitatory neurons (E→E synapses) in the mouse hippocampus and are considered to be the mechanical adhesion sites between axon terminals and dendritic shafts. However, it remains unclear whether they are present at other types of synapses, such as glutamatergic synapses on GABAergic inhibitory neurons (E→I synapses) and GABAergic synapses on excitatory neurons (I→E synapses) and inhibitory neurons (I→I synapses). We showed here that the PAJ components, such as nectin-1, nectin-3, l-afadin, N-cadherin, β-catenin, and αN-catenin, were observed at all four types of synapses in cultured mouse hippocampal neurons. In the adult mouse hippocampus, these PAJ components were observed at a subset of I→I synapses on parvalbumin-positive GABAergic inhibitory neurons, similarly to their presence at E→E synapses in the CA1 and CA3 regions. In contrast, several PAJ components, including nectin-3, l-afadin, N-cadherin, β-catenin, and αN-catenin, were observed at E→I and I→E synapses, whereas nectin-1 was absent. These results indicate that the PAJs are formed at a subset of I→I synapses in addition to E→E synapses, where all examined PAJ components are present, whereas E→I and I→E synapses exhibit only partial localization of these components, reflecting molecular diversity among different synapses in the adult mouse hippocampus. - Source: PubMed
Katanazaka KimitakaShiotani HajimeMiyata MuneakiKameyama TakeshiKedashiro ShinKomaki RyouheiNishii ShotaKashiwagi YutaroSato YukaOkabe ShigeoChihara NorioMatsumoto RikiMizutani KiyohitoTakai Yoshimi - Herpes simplex encephalitis (HSE) is a life-threatening disease of the central nervous system caused by herpes simplex virus type 1 (HSV-1). Despite being a standard treatment, antiviral acyclovir and its derivatives often face limitations in clinical application due to their side effects and viral drug resistance. Inspired by viral entry through recognition of nectin-1 on the host cell surface, we engineered enucleated mesenchymal stem cells with high nectin-1 expression (eMSCs) to serve as "decoys" for capturing HSV-1. We found that eMSCs competitively captured the virus in the presence of neurons while inhibiting its replication and spread by removing the nucleus in advance. Interestingly, due to the absence of nuclei, eMSCs capturing the virus trigger macrophage efferocytosis through intrinsic apoptosis after approximately 60 h, thereby accelerating existing viral clearance. This is a property lacking in current antiviral drugs, including ACV. In summary, this strategy significantly improved the quality of life of HSE mice. - Source: PubMed
Publication date: 2026/03/12
Zhou LeiSong QingyingCao MengnianQin MengjiaoWang ZhenyaSun YiwenXue DayuZhang ZhenzhongShi JinjinLiu Junjie - Herpes simplex virus 1 (HSV-1) entry is a complex interplay of viral and host factors. The mechanisms of its regulation remain undefined. HSV-1 entry occurs via multiple distinct and cell-type dependent pathways, further complicating study of this process. HSV-1 strains with atypical entry properties aid in the elucidation of entry determinants. HSV-1 strain ANG path exhibits entry in Vero cells at 4 °C, whereas wild-type strains do not. We investigated the determinants of low temperature entry by HSV-1 ANG path in several cell types. The receptor nectin-2 mediated 4 °C entry of HSV-1 ANG path into CHO-K1 cells, but the related receptor nectin-1 did not, suggesting that gD-binding receptors are a determinant of HSV-1 entry at low temperatures. In HaCaT cells, both HSV-1 ANG path and wild-type strain KOS entered at 4 °C, while HSV-1 chimera 27/III, which contains KOS strain gB in the ANG path virus background, did not. This suggests that gB functions as a determinant of low temperature entry of HSV-1. Together, the findings suggest that there are multiple determinants and mechanisms of HSV-1 low temperature entry and that the requirements differ by cell type. - Source: PubMed
Publication date: 2026/01/27
Lynch Colleen MHull McKenna ANicola Anthony V