HTNV gp Specific Neutra™ Antibody Products

Hantaan virus (HTNV), categorized within the Orthohantavirus genus of the Hantaviridae family, primarily transmits to humans through inhalation of airborne particles derived from rodent excretions. As the principal etiological agent of Hemorrhagic Fever with Renal Syndrome (HFRS), HTNV induces serious clinical manifestations such as pyrexia, acute renal insufficiency, and hemorrhagic complications. Structurally, the virion comprises an outer envelope encapsulating a tripartite, negative-sense RNA genome organized into distinct S, M, and L segments. The M segment exclusively encodes Gn and Gc glycoproteins, which act as indispensable mediators of host cell invasion. These membrane-bound proteins integrate into the viral envelope's lipid layer, creating an organized surface pattern. Biosynthesis initiates through a precursor polyprotein that undergoes enzymatic cleavage to produce functional Gn and Gc units.

Fig. 1 The HTNV virion.¹

Structure of HTNV gp

Functioning as type I transmembrane proteins, HTNV's Gn and Gc govern critical virus-host interactions. Production begins as a unified polypeptide chain that simultaneously enters the endoplasmic reticulum during translation. Within this organelle, carbohydrate attachments and structural refinements occur before cellular proteases cleave the precursor into distinct Gn and Gc molecules. Following dimerization, these glycoproteins migrate through the Golgi complex, acquiring additional sugar modifications prior to membrane targeting. During viral assembly, the proteins embed into developing particles, constructing surface projections through the assembly of four Gn-Gc dimers into a quaternary complex.

Fig. 2 Schematic representation of HTNV gp processing.²

Roles of HTNV gp in Virus Cell Entry

Viral penetration involves coordinated actions of Gn and Gc through three sequential phases:

• Receptor Recognition: Initial attachment involves Gn-mediated engagement with host membrane receptors, with receptor specificity dictating cellular tropism. This interaction induces intracellular signaling cascades that prime the cell for viral entry.
• Endocytic Internalization: Cellular uptake occurs via multiple endocytic routes, including clathrin-dependent pathways and macropinocytosis. The selected entry mechanism impacts subsequent vesicular trafficking and infection kinetics. Endosomal maturation following internalization creates environmental conditions necessary for membrane fusion.
• Membrane Fusion: Acidification of endocytic vesicles induces structural rearrangements in Gc glycoproteins. Exposure of fusion peptides enables Gc-mediated merger of viral and endosomal membranes, establishing continuity between viral contents and cytoplasmic components to initiate replication processes.

Fig. 3 HTNV gp in the virus life cycle.²

Roles of HTNV gp in Virus Cell Exit

Beyond facilitating entry, HTNV glycoproteins coordinate particle assembly and release. Post-replication trafficking directs newly synthesized Gn and Gc to plasma membrane domains where interaction with viral ribonucleoprotein complexes occurs. The cytoplasmic domains of these glycoproteins mediate selective packaging of genomic material into budding structures. Through membrane curvature induction and scission activities, Gn-Gc complexes drive protrusion formation and subsequent virion detachment. This egress mechanism ensures dissemination of infectious particles capable of propagating infection.

Antibodies Targeting HTNV gp

Antibodies targeting HTNV glycoproteins serve vital functions in both neutralizing viral particles and stimulating protective immunological defenses. Through their interaction with Gn or Gc antigenic sites, these antibodies obstruct receptor binding, prevent membrane fusion events, or hinder cellular entry mechanisms. Such neutralizing antibodies represent indispensable tools for investigating HTNV disease progression and facilitating the development of therapeutic interventions and prophylactic vaccines. For example, research has characterized monoclonal antibodies that recognize distinct structural regions on Gn and Gc, offering mechanistic clarity regarding molecular-level neutralization processes.

Creative Biolabs offers a variety of anti-HTNV gp antibody products to assist you with your HTNV infection research. Our antibodies are suitable for various applications, including ELISA, WB, and neutralization assays. These high-quality products provide specific and reliable results, helping you to advance your research.

REFERENCES

1. Meier, Kristina, et al. "Hantavirus replication cycle—An updated structural virology perspective." Viruses 13.8 (2021): 1561. Distributed under Open Access license CC BY 4.0, without modification. https://doi.org/10.3390/v13081561
2. Cifuentes-Muñoz, Nicolás, Natalia Salazar-Quiroz, and Nicole D. Tischler. "Hantavirus Gn and Gc envelope glycoproteins: key structural units for virus cell entry and virus assembly." Viruses 6.4 (2014): 1801-1822. Distributed under Open Access license CC BY 3.0, without modification. https://doi.org/10.3390/v6041801