CD112 _ Nectin_2 _ PVRL2 Antibody
- Known as:
- CD112 _ Nectin_2 _ PVRL2 Antibody
- Catalog number:
- 10005-R005
- Product Quantity:
- 100
- Category:
- -
- Supplier:
- Smart Serology
- Gene target:
- CD112 _ Nectin_2 PVRL2 Antibody
Related genes to: CD112 _ Nectin_2 _ PVRL2 Antibody
- Gene:
- NECTIN2 NIH gene
- Name:
- nectin cell adhesion molecule 2
- Previous symbol:
- HVEB, PVRL2
- Synonyms:
- PVRR2, PRR2, CD112
- Chromosome:
- 19q13.32
- Locus Type:
- gene with protein product
- Date approved:
- 1999-11-15
- Date modifiied:
- 2016-02-12
- Gene:
- PVRIG NIH gene
- Name:
- PVR related immunoglobulin domain containing
- Previous symbol:
- -
- Synonyms:
- MGC2463, C7orf15, CD112R
- Chromosome:
- 7q22.1
- Locus Type:
- gene with protein product
- Date approved:
- 2006-09-20
- Date modifiied:
- 2017-09-14
Related products to: CD112 _ Nectin_2 _ PVRL2 Antibody
Related articles to: CD112 _ Nectin_2 _ PVRL2 Antibody
- Nectin and nectin-like proteins are cell adhesion molecules belonging to the immunoglobulin superfamily that also play a crucial role in the process of immune modulation by interacting with immune receptors like TIGIT, DNAM-1, CD96 and PVRIG. Nectin-4 is a tumour-specific antigen that interacts exclusively with the inhibitory immune receptor TIGIT, resulting in inhibition of NK-cell cytotoxicity and facilitating the process of immune evasion by the cancer cells in the tumour microenvironment. Therefore, deciphering the molecular and structural mechanisms underlying this novel interaction can provide insights for the development of targeted immunotherapeutic interventions. In this study, using structure-guided mutagenesis studies, a novel TIGIT mutant is engineered exhibiting enhanced interaction affinity towards nectin-4 and reduced binding to other TIGIT ligands, such as PVR and nectin-2, which, in contrast to nectin-4, are predominantly expressed on healthy cells. Surface plasmon resonance-based biophysical studies were done to characterize and compare the interaction kinetics of the wild-type (WT) and the engineered mutant TIGIT ectodomains with their ligands. We have shown how a single point mutation of an amino acid residue located in the centre of the F strand of TIGIT dictates its interaction affinity with its ligand. These findings can provide a framework for the development of small-sized non-antibody therapeutics specifically targeted towards nectin-4 overexpressing cancer cells with minimal off-target effects on healthy cells. - Source: PubMed
Ganguli NamrataShaw SayantanSarkar SohiniGoswami SaumyadeepMukherjee GayatriSamanta Dibyendu - Preeclampsia is characterized by hypertension and proteinuria after the 20th week of pregnancy. The disease is divided into early and late onset according to the time of diagnosis. Early onset preeclampsia (EOP) develops after the 20th week of pregnancy. The late-onset form usually occurs after the 34th week of pregnancy. TIGIT and PVRIG are immune checkpoint inhibitor receptors. PVRIG binds only to the PVRL2 (nectin-2, CD112). TIGIT binds to both CD112 and CD155. In our study, the control group consisted of placentas from healthy pregnant women, the early onset preeclampsia group (EOP) consisted of patients diagnosed before the 34th week, and the late-onset preeclampsia group (LOP) consisted of placentas from patients diagnosed at or after the 34th week. TIGIT, PVRIG, CD155, and CD112 expression in placental materials was evaluated both immunohistochemically and by RT-PCR. As a result of H scoring of immunohistochemical expression, it was observed that CD112 and CD155 expression decreased and PVRIG expression increased when the EOP and LOP groups were compared with the control group. In the early onset preeclampsia group, CD112, CD155, TIGIT, and PVRIG gene expression increased twofold compared to that in the control group. In the late-onset preeclampsia group, the expression of all the genes decreased to one-third. The results of our study revealed that these genes may serve as biomarkers for early- and late-onset preeclampsia. Detailed studies are required to determine the use of these receptors in the diagnosis and treatment of the disease. - Source: PubMed
Publication date: 2025/05/28
Çetin HülyaLafcı İlknurArman Karakaya YelizEr Urgancı BuketKoşar Can Özlem - The immune checkpoint protein, CD112 receptor (CD112R, also known as PVRIG), suppresses T and natural killer (NK) cell activation upon binding to tumor-expressed CD112 (Nectin-2) ligands. Here, we determine the structure of the CD112-CD112R complex and use it to guide the engineering of multiple CD112-targeting immunotherapy candidates. The 2.2 Å-resolution crystal structure reveals an antiparallel, lock-and-key binding mode in which CD112R disrupts CD112 homodimerization. Structural analysis informed directed evolution campaigns focused on remodeling the CD112-CD112R interface, resulting in the isolation of CD112R mutants with greatly increased expression and CD112-binding affinity. The highest-affinity variant, CD112R, potently inhibits CD112-CD112R interactions when utilized as a soluble CD112 trap. Furthermore, incorporating CD112R variants into chimeric antigen receptors (CARs) and T cell engagers (TCEs) leads to more robust T cell activation and killing of CD112 triple-negative breast cancer (TNBC) cells compared with wild-type CD112R. This strategy demonstrates how structural insights can be leveraged to efficiently generate panels of "affinity-tuned" biologics for immunotherapy. - Source: PubMed
Publication date: 2025/04/24
Singh SrishtiJulia EstefaniaKalita ParismitaMason CharlotteMing QianqianLee-Sam AnsarGordon SumaiBuitrago Maria EmiliaLeung Daisy WHwu PatrickLuca Vincent C - Nectin and nectin-like (Necl) co-receptor axis, comprised of receptors DNAM-1, TIGIT, CD96, PVRIG, and nectin/Necl ligands, is gaining prominence in immuno-oncology. Within this axis, the inhibitory receptor PVRIG recognizes Nectin-2 with high affinity, but the underlying molecular basis remains unknown. By determining the crystal structure of PVRIG in complex with Nectin-2, we identified a unique CC' loop in PVRIG, which complements the double-lock-and-key binding mode and contributes to its high affinity for Nectin-2. The association of the corresponding charged residues in the F-strands explains the ligand selectivity of PVRIG toward Nectin-2 but not for Necl-5. Moreover, comprehensive comparisons of the binding capacities between co-receptors and ligands provide innovative insights into the intra-axis immunoregulatory mechanism. Taken together, these findings broaden our understanding of immune recognition and regulation mediated by nectin/Necl co-receptors and provide a rationale for the development of immunotherapeutic strategies targeting the nectin/Necl axis. - Source: PubMed
Publication date: 2024/04/15
Hu SongtaoHan PuWang MeiyuCao XiaoqingLiu HaoZhang ShuailongZhang ShuijunLiu JunHan YiXiao JinheChen QiangMiao KaiQi JianxunTan ShuguangGao George FuWang Han - Poliovirus receptor-related 2 (PVRL2, also known as nectin-2 or CD112) is believed to act as an immune checkpoint protein in cancer; however, most insight into its role is inferred from studies on its known receptor, poliovirus receptor (PVR)-related immunoglobulin domain protein (PVRIG, also known as CD112R). Here, we study PVRL2 itself. PVRL2 levels were found to be high in tumor cells and tumor-derived exosomes. Deletion of PVRL2 in multiple syngeneic mouse models of cancer showed a dramatic reduction in tumor growth that was immune dependent. This effect was even greater than that seen with deletion of PD-L1. PVRL2 was shown to function by suppressing CD8+ T and natural killer cells in the tumor microenvironment. The loss of PVRL2 suppressed tumor growth even in the absence of PVRIG. In contrast, PVRIG loss showed no additive effect in the absence of PVRL2. T-cell immunoreceptor with Ig and ITIM domains (TIGIT) blockade combined with PVRL2 deletion resulted in a near complete block in tumor growth. This effect was not recapitulated by the combined deletion of PVRL2 with its paralog, PVR, which is the ligand for TIGIT. These data uncover PVRL2 as a distinct inhibitor of the antitumor immune response with functions beyond that of its known receptor PVRIG. Moreover, the data provide a strong rationale for combinatorial targeting of PVRL2 and TIGIT for cancer immunotherapy. - Source: PubMed
Yang JiulingWang LiByrnes James RKirkemo Lisa LDriks HannahBelair Cassandra DAguilar Oscar ALanier Lewis LWells James AFong LawrenceBlelloch Robert