98%
921
2 minutes
20
The spike glycoprotein is a key factor in the infection cycle of SARS-CoV-2, as it mediates both receptor recognition and membrane fusion by the virus. Therefore, in this study, we aimed to design a multi-peptide conjugate vaccine against SARS-CoV-2, targeting the early stages of the virus's life cycle. We used iBoost technology, which is designed to induce immune responses against low- or non-immunogenic epitopes. We selected six peptide sequences, each representing a key domain of the spike protein (i.e., receptor binding domain (RBM), subdomain 1 (SD1), subdomain 2 (SD2), S1/S2, fusion peptide and the S2' sequences (FP + S2'), heptad repeat 1 (HR1)). Immunization studies in mice displayed targeted humoral and cellular immune responses against specific peptides of the spike protein simultaneously, while inducing cross-protection against the Delta and Omicron coronavirus variants. Moreover, vaccinated hamsters challenged with SARS-CoV-2 elicited high antibody levels against key peptides, induced early neutralizing antibody responses and resulted in less weight loss compared to controls. This highlights the potential for improving viral control and disease outcomes when utilizing this strategy. Therefore, by using iBoost technology in conjunction with our peptide design strategy, we were able to successfully target non-immunodominant regions in the spike protein while activating both arms of the adaptive immune system.
Download full-text PDF |
Source |
---|---|
http://dx.doi.org/10.1016/j.vaccine.2025.126989 | DOI Listing |
Phys Chem Chem Phys
September 2025
School of Chemistry and Chemical Engineering, University of Jinan, Jinan 250022, P. R. China.
The COVID-19 pandemic remains a global health crisis, with successive SARS-CoV-2 variants exhibiting enhanced transmissibility and immune evasion. Notably, the Omicron variant harbors extensive mutations in the spike protein's receptor-binding domain (RBD), altering viral fitness. While temperature is a critical environmental factor modulating viral stability and transmission, its molecular-level effects on variant-specific RBD-human angiotensin-converting enzyme 2 (hACE2) interactions remain underexplored.
View Article and Find Full Text PDFInfluenza Other Respir Viruses
September 2025
Department of Medical Laboratory, The Affiliated Hospital of Shaanxi University of Chinese Medicine, Xianyang, China.
Objectives: This study compared the diagnostic accuracy of seven different commercial serological assays for COVID-19, using RT-PCR as the gold standard, through meta-analysis and indirect comparison.
Methods: Fifty-seven studies, published from November 2019 to June 2024, were included. The diagnostic performance of IgA, IgG, and total antibody assays for SARS-CoV-2 was assessed.
Antiviral Res
September 2025
Department of Immunology and Pathogen Biology, Key Laboratory of Pathogen and Host-Interactions, Ministry of Education, School of Medicine, Tongji University, Shanghai, 200331, China. Electronic address:
DMBT1 is a large scavenger receptor cysteine rich (SRCR) B protein that has been reported as a tumor suppressor gene and a co-receptor for HIV-1 infection. Here, we found DMBT1 is a major mucosal protein bound to SARS-CoV-2. Overexpression of DMBT1 in 293T cells may enhanced infection by SARS-CoV-2 in ACE2 dependent manner.
View Article and Find Full Text PDFbioRxiv
August 2025
Department of Integrative Structural and Computational Biology, The Scripps Research Institute, La Jolla, CA 92037, USA.
Extensive mutations in SARS-CoV-2 spike protein have rendered most therapeutic monoclonal antibodies (mAbs) ineffective. However, here we describe VYD222 (pemivibart), a human mAb re-engineered from ADG20 (adintrevimab), which maintains potency despite substantial virus evolution. VYD222 received FDA Emergency Use Authorization for pre-exposure prophylaxis of COVID-19 in certain immunocompromised adults and adolescents.
View Article and Find Full Text PDFAdv Sci (Weinh)
September 2025
Department of Chemistry and Biochemistry, University of California San Diego, La Jolla, CA, 92093-0359, USA.
Discovery of therapeutic antibodies against infectious disease pathogens presents distinct challenges. Ideal candidates must possess not only the properties required for any therapeutic antibody (e.g.
View Article and Find Full Text PDF