Database of articles cited by EMDB/PDB/SASBDB data

Keywords
Structure methods	All X-ray diffraction NMR electron microscopy small angle scattering neutron diffraction fiber diffraction powder diffraction infrared spectroscopy EPR fluorescence transfer theoretical model Hybrid
Author
Journal
IF	>30 >20 >10 >5 all

Title	Monoclonal neutralizing antibodies elicited by infection with Kaposi sarcoma-associated herpesvirus reveal critical sites of vulnerability on gH/gL.
Journal, issue, pages	PLoS Pathog, Vol. 22, Issue 1, Page e1013772, Year 2026
Publish date	Jan 7, 2026
Authors	Yu-Hsin Wan / Sara Pernikoff / Nicholas T Aldridge / Kevin Lang / Holly M Dudley / Samuel C Scharffenberger / Gargi Kher / Warren Phipps / Marie Pancera / Jim Boonyaratanakornkit / Andrew T McGuire /
PubMed Abstract	Kaposi sarcoma-associated herpesvirus (KSHV) is an oncogenic virus that causes Kaposi sarcoma, primary effusion lymphoma and multicentric Castleman disease. A vaccine that prevents KSHV infection or ...Kaposi sarcoma-associated herpesvirus (KSHV) is an oncogenic virus that causes Kaposi sarcoma, primary effusion lymphoma and multicentric Castleman disease. A vaccine that prevents KSHV infection or serves in the treatment of KSHV-related diseases represents a critical unmet need, however, the types of immune responses a vaccine should elicit have not been well defined. The gH/gL glycoprotein complex is an important target of KSHV-neutralizing antibodies, but the epitope specificities targeted by these antibodies remain unknown. Here, we isolated 12 gH/gL-specific monoclonal antibodies (mAbs) from KSHV-infected donors and performed structure/function analyses. These mAbs bind recombinant gH/gL with nanomolar affinities and epitope binning analyses revealed that the mAbs bind to 5 epitope clusters on gH/gL. Seven mAbs were able to neutralize KSHV infection of epithelial cell lines. Two potent neutralizing mAbs mapped to the EphA2 binding site as determined by inhibition of the receptor-ligand interaction and negative stain electron microscopy (nsEM) of the mAb/gH/gL complex. The epitopes of other neutralizing mAbs targeting novel sites of vulnerability were determined by a combination of cryogenic electron microscopy and nsEM. Together, these mAbs help to define the relevant epitope targets for KSHV vaccine design, have utility in understanding the role of antibodies in preventing KSHV infection, enable the development of immunotherapy approaches, and provide valuable tools to understand the molecular details of the KSHV entry process.
External links	PLoS Pathog / PubMed:41499715 / PubMed Central
Methods	EM (single particle)
Resolution	3.51 - 24.15 Å
Structure data	EMDB-72129: Negative Stain EM map of KSHV glycoprotein gH and gL Method: EM (single particle) / Resolution: 7.23 Å EMDB-72130: Negative Stain EM map of KSHV glycoprotein gHgL in complex with MLKH1 FAB Method: EM (single particle) / Resolution: 15.6 Å EMDB-72131: Negative Stain EM map of KSHV glycoprotein gHgL in complex with MLKH5 FAB Method: EM (single particle) / Resolution: 16.6 Å EMDB-72132: Negative Stain EM map of KSHV glycoprotein gHgL in complex with MLKH5, MLKH10 and MLKH3 FABs. Method: EM (single particle) / Resolution: 16.9 Å EMDB-72133: Negative Stain EM map of KSHV glycoprotein gHgL in complex with MLKH5, MLKH10 and MLKH6 FABs Method: EM (single particle) / Resolution: 24.15 Å EMDB-72525: Negative Stain EM map of KSHV glycoprotein gHgL in complex with MLKH5 , MLKH10 and MLKH12 FABs. Method: EM (single particle) / Resolution: 23.07 Å 73789 9z3q EMDB-73789, PDB-9z3q: Cryo-EM structure of KSHV glycoprotein gHgL in complex with MLKH3 and MLKH10 FABs Method: EM (single particle) / Resolution: 3.51 Å
Source	human gammaherpesvirus 8 mus musculus (house mouse) Homo sapiens (human)
Keywords	IMMUNE SYSTEM / KSHV / glycoprotein / Antibody