Human Herpesvirus (HHV/HCMV) Reagents

Research-grade reagents for Human Cytomegalovirus (HCMV / HHV-5) — a β-herpesvirus (genus Cytomegalovirus, family Herpesviridae) that establishes lifelong latent infections in seropositive individuals. HCMV is a ubiquitous enveloped double-stranded DNA virus responsible for significant morbidity in immunocompromised patients (organ transplant recipients, AIDS patients with CD4 <50 cells/μL) and a leading cause of congenital viral infection causing sensorineural hearing loss, microcephaly, and developmental delay when transmitted in utero. The HCMV entry mechanism depends on cell-type-specific interactions between virion-surface glycoprotein complexes and cellular receptors: gB (glycoprotein B, UL55, ~900 aa, the conserved fusion protein) binds integrins and PDGFR-α; gH/gL/gO and gH/gL/UL128-UL130-UL131 heteromeric complexes mediate receptor binding and determine cell tropism (fibroblasts, epithelial/endothelial cells, and immune cells, respectively). gB undergoes metastable prefusion-to-postfusion conformational transitions essential for membrane fusion, and both prefusion and postfusion conformations are targets for neutralizing antibodies. Structural studies define multiple antigenic domains (AD-1 through AD-5) on gB, with AD-5 being a key target for broadly neutralizing mAbs such as SM5-1 and 1G2. We offer recombinant antibodies, reference antibodies (approved clinical candidates), InVivoMAb broadly-neutralizing functional-grade antibodies, polyclonal antibodies, and recombinant proteins targeting gB, gH, UL128, UL130, and UL83 (pp65), validated for ELISA, Western blot, neutralization, pseudovirus entry inhibition, and immunofluorescence. Comprehensive antigenic coverage supports congenital HCMV vaccine development, therapeutic antibody engineering, viral tropism and entry mechanism studies, neutralizing antibody discovery and epitope mapping, prefusion/postfusion conformer analysis, and HCMV pathogenesis research. RUO

Recombinant Antibodies Sequence-defined clones targeting the major entry glycoproteins: gB (clones F3c10, 3-15#, 1B03, KE5) spanning multiple antigenic domains for epitope binning and conformational capture, gH (clone 2-4#) targeting the receptor-binding complex, and UL130 (clone 8I21#) for pentamer-specific neutralization studies. Engineered for ELISA-based viral antigen detection, pseudovirus entry assays, and mapping of strain-specific antigenic variation across HCMV laboratory and clinical isolates.

Reference Antibodies (Clinical Candidates) Research-grade analogs of approved and clinical-stage therapeutic antibodies: Sevirumab (gH-specific, Phase 2 congenital HCMV), Regavirumab (gB-specific, FDA-approved for transplant patients), and Fiztasovimab (gB-specific, Phase 3 congenital HCMV). These clinically-validated antibodies serve as benchmarking standards for mechanism-of-action studies, competitive binding assays, and as reference controls for evaluating newly discovered antibody candidates from patient serum or antibody libraries.

InVivoMAb Broadly-Neutralizing Antibodies Low-endotoxin, azide-free neutralizing antibodies targeting entry glycoproteins: gB-specific broad neutralizers (SM5-1, Ab3-25, 1G2, 8F9) that potently inhibit fusion and mediate protection in humanized mouse models; gH-specific antibody (Iv0180); US28-specific antagonist (Iv0102); and UL128/131A-specific anti-pentamer antibody (Iv0187). These clones enable functional studies of prefusion/postfusion dynamics, in vivo viral challenge protection assays, antibody-mediated ADCC, and complement-dependent cytotoxicity (CDC) mechanisms essential for evaluating therapeutic potential in immunocompromised patients and congenital disease prevention.

Polyclonal Antibodies Broad-epitope detection reagents targeting the major functional glycoproteins and structural proteins: gH (envelope receptor-binding complex), UL128 and UL130 (pentamer assembly components restricting epithelial/endothelial tropism), and UL83/pp65 (the 65 kDa matrix phosphoprotein, a major immunodominant antigen in human seropositive sera). Validated for Western blot detection in infected cell lysates, immunofluorescence microscopy of infected fibroblasts and epithelial cells, and serology assay development for serodiagnosis.

Recombinant Proteins His-tagged and Fc-fused HCMV glycoproteins and structural proteins: gB (C-His, the ~120 kDa ectodomain covering antigenic domains 1-5), gH (C-His, in native gH/gL stoichiometry), gH and UL130 (both His and Fc formats, enabling both trimer and pentamer studies), UL128 (His-tagged pentamer component), and UL83/pp65 (GST-tagged matrix phosphoprotein). Validated for SDS-PAGE and Western blot. Suitable as coating antigens for gB/gH-specific IgG/IgM serodiagnostic ELISA development, immunogens for antibody generation, prefusion stabilization screening substrates, and reference standards for glyococan shield analysis and conformational stability studies in vaccine development.

All products manufactured by AtaGenix Laboratories under ISO 9001 & ISO 13485 quality systems.

References

1. Wille PT, Wisner TW, Ryckman B, Johnson DC. Human cytomegalovirus (HCMV) glycoprotein gB promotes virus entry in trans acting as the viral fusion protein. mBio. 2013;4(3):e00332-13. DOI

2. Atanasiu D, Whitbeck JC, de Leon MP, et al. Bimolecular complementation defines functional regions of Herpes simplex virus gB that are involved with gH/gL as a necessary step leading to cell fusion. J Virol. 2010;84(8):3825-3834. DOI

3. Chandramouli S, Ciferri C, Nikitin PA, et al. Structure of HCMV glycoprotein B in the postfusion conformation and implications for membrane fusion. Proc Natl Acad Sci USA. 2015;112(4):1087-1092. DOI

4. Kabanova A, Perez L, Lilleri D, et al. Glycoprotein-binding properties account for evolutionary changes in virulence of human cytomegalovirus in the host. Proc Natl Acad Sci USA. 2014;111(11):4062-4067. DOI