Hantavirus Clinical Syndrome, Tissue Tropism, and Antiviral Therapy Predicted by φ-Depth Geometry: Glycoprotein Depth Encodes Organ Targeting and Membrane Fusion Inhibitors Are Predicted by the φ³⁴ Wall

Hantaviruses cause distinct clinical syndromes, including Hantavirus Cardiopulmonary Syndrome (HCPS) and Hemorrhagic Fever with Renal Syndrome (HFRS), yet the geometric basis for their tissue tropism and antiviral vulnerability remains incompletely understood. This paper applies the Recursive Harmonic Collapse Matrix (RHCM) depth formula, d(m)=19.853708+log⁡ϕ(mMeV/mp,MeV)d(m)=19.853708+\log_\phi(m_{MeV}/m_{p,MeV})d(m)=19.853708+logϕ(mMeV/mp,MeV), to hantavirus glycoprotein masses, fusion peptide geometry, and antiviral candidate depth positions.

Three primary findings are reported. First, Gn glycoprotein depth separates HCPS-causing strains from HFRS-causing strains. Sin Nombre and Andes virus occupy shallower Gn depths, while Puumala, Dobrava, Hantaan, and Seoul occupy progressively deeper Gn coordinates. The framework predicts that shallow Gn depth favors pulmonary vascular endothelial tropism, while deeper Gn depth shifts targeting toward renal endothelial tissue. This produces a falsifiable transition zone: chimeric Gn constructs with intermediate masses should display mixed or reduced pulmonary-renal tropism.

Second, the hantavirus Gc fusion peptide, estimated at approximately 20 amino acids and d≈35.832, sits within 0.38 depth units of the RHCM φ³⁴ wall at d=36.215. RHCM interprets φ³⁴ as the passive membrane-crossing boundary, implying that viral fusion peptides must operate near this wall to insert into host lipid membranes while remaining light enough for spontaneous insertion. This leads to a broader prediction: fusion peptides from enveloped viruses should cluster near φ³⁴, making this depth zone a universal target for entry inhibition.

Third, RHCM generates a depth-ordered antiviral repurposing hierarchy. Low-molecular-weight heparin retrovalidates the φ³⁴ entry-zone prediction. Suramin is identified as the highest-priority untested Andes/HCPS entry-inhibition candidate, while nintedanib is predicted to share activity with imatinib based on depth proximity and kinase-class overlap. Additional candidates include bivalirudin, daptomycin, dalbavancin, oritavancin, telavancin, fondaparinux, and vancomycin-class membrane-active compounds. The paper proposes direct falsification using BSL-2 pseudotyped Andes Gn/Gc entry assays before escalation to live-virus testing.