35B5 for COVID-19

c19early.org

COVID-19 Treatment Clinical Evidence

COVID-19 involves the interplay of 500+ viral and host proteins and factors, providing many therapeutic targets. c19early analyzes 6,000+ studies for 220+ treatments—over 17 million hours of research. Only three high-profit early treatments are approved in the US. In reality, many treatments reduce risk, with 25 low-cost treatments approved across 163 countries.

Naso/oropharyngeal treatment Effective Treatment directly to the primary source of initial infection.
Healthy lifestyles Protective Exercise, sunlight, a healthy diet, and good sleep all reduce risk.
Immune support Effective Vitamins A, C, D, and zinc show reduced risk, as with other viruses.
Thermotherapy Effective Methods for increasing internal body temperature, enhancing immune system function.
Systemic agents Effective Many systemic agents reduce risk, and may be required when infection progresses.
High-profit systemic agents Conditional Effective, but with greater access and cost barriers.
Monoclonal antibodies Limited Utility Effective but rarely used—high cost, variant dependence, IV/SC admin.
Acetaminophen Harmful Increased risk of severe outcomes and mortality.
Remdesivir Harmful Increased mortality with longer followup. Increased kidney and liver injury, cardiac disorders.

35B5 may be beneficial for COVID-19 according to the studies below. COVID-19 involves the interplay of 500+ viral and host proteins and factors providing many therapeutic targets. Scientists have proposed 12,000+ potential treatments. c19early.org analyzes 220+ treatments. We have not reviewed 35B5 in detail.

Studies suggesting benefit with 35B5

Wei et al., An IgG-like fusion protein comprising an anti-spike S2 antibody and ACE2 exhibits potent and broad neutralization against SARS-CoV-2 and variants of concern, Antibody Therapeutics, doi:10.1093/abt/tbag041

Abstract Background The continuous evolution of severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) highlights the value of broad-spectrum antiviral strategies. Antibody-engineering approaches targeting conserved regions of the Spike protein may enhance neutralizing potency and breadth. Methods A human antibody (P23) against the Spike protein of SARS-CoV-2 was identified using a human antibody phage display library panning and screening for binding affinity and breadth against multiple coronavirus Spike proteins using surface plasmon resonance (SPR). The epitope of P23 was characterized using the S1 and S2 subunits of SARS-CoV-2 Spike protein and hydrogen–deuterium exchange mass spectrometry (HDX-MS). An IgG–like bispecific fusion protein (Bs-ACE2-P23) was engineered by fusing the extracellular domain (ECD) of human angiotensin-converting enzyme 2 (ACE2) to the N-terminus of the P23 heavy chain (HC). Neutralizing activity was evaluated against both pseudotyped and authentic SARS-CoV-2 variants. Results P23 cross-bound Spike proteins from SARS-CoV-2 wild type (WT), D614G and JN.1 variants, Pangolin-CoV, Bat coronavirus RaTG13, and SARS-CoV-1, recognizing an epitope on the S2 subunit adjacent to the fusion peptide (FP). While P23 was ineffective against D614G-containing SARS-CoV-2 variants, Bs-ACE2-P23 exhibited markedly enhanced neutralization potency. This bispecific architecture also improved the neutralizing activity of another FP-targeting antibody. Conclusion We developed a bispecific fusion protein with potent broad-spectrum neutralizing activity against SARS-CoV-2 variants. This architecture provides a promising strategy for next-generation coronavirus biologics.

Bhasin et al., CoV-UniBind: a unified antibody binding database for SARS-CoV-2, Bioinformatics Advances, doi:10.1093/bioadv/vbaf328

Abstract Summary Since the emergence of SARS-CoV-2, numerous studies have investigated antibody interactions with viral variants in vitro, and several datasets have been curated to compile available protein structures and experimental measurements. However, existing data remain fragmented, limiting their utility for the development and validation of machine learning models for antibody–antigen interaction prediction. Here, we present CoV-UniBind, a unified database comprising over 75 000 entries of SARS-CoV-2 antibody–antigen sequence, binding, and structural data, integrated and standardized from three public sources and multiple peer-reviewed publications. To demonstrate its utility, we benchmarked multiple protein folding, inverse folding, and language models across tasks relevant to antibody design and vaccine development. We expect CoV-UniBind to facilitate future computational efforts in antibody and vaccine development against SARS-CoV-2. Availability and implementation The curated datasets, model scores and antibody synonyms are free to download at https://huggingface.co/datasets/InstaDeepAI/cov-unibind. Folded structures are available upon request.

Nocini et al., Improving Nasal Protection for Preventing SARS-CoV-2 Infection, Biomedicines, doi:10.3390/biomedicines10112966

Airborne pathogens, including SARS-CoV-2, are mainly contracted within the airway pathways, especially in the nasal epithelia, where inhaled air is mostly filtered in resting conditions. Mucosal immunity developing after SARS-CoV-2 infection or vaccination in this part of the body represents one of the most efficient deterrents for preventing viral infection. Nonetheless, the complete lack of such protection in SARS-CoV-2 naïve or seronegative subjects, the limited capacity of neutralizing new and highly mutated lineages, along with the progressive waning of mucosal immunity over time, lead the way to considering alternative strategies for constructing new walls that could stop or entrap the virus at the nasal mucosa surface, which is the area primarily colonized by the new SARS-CoV-2 Omicron sublineages. Among various infection preventive strategies, those based on generating physical barriers within the nose, aimed at impeding host cell penetration (i.e., using compounds with mucoadhesive properties, which act by hindering, entrapping or adsorbing the virus), or those preventing the association of SARS-CoV-2 with its cellular receptors (i.e., administering anti-SARS-CoV-2 neutralizing antibodies or agents that inhibit priming or binding of the spike protein) could be considered appealing perspectives. Provided that these agents are proven safe, comfortable, and compatible with daily life, we suggest prioritizing their usage in subjects at enhanced risk of contagion, during high-risk activities, as well as in patients more likely to develop severe forms of SARS-CoV-2 infection.