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David versus goliath: ACE2-Fc receptor traps as potential SARS-CoV-2 inhibitors

MABS (2022)

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Summary: Researchers constructed an ACE2-human IgG1 fusion protein with mutations in the catalytic domain of ACE2, which significantly increased binding to SARS-CoV-2 spike protein and improved lung infection caused by the virus in vivo. This study suggests that MDR504 hACE2-Fc may be a promising candidate for the treatment or prevention of COVID-19 and emerging variants.

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Summary: The COVID-19 pandemic has created a public health crisis, leading to the urgent development of therapeutic treatments and virus detection methods. Monoclonal antibodies (mAbs) have emerged as powerful tools for treating and detecting diseases due to their high specificity and reliability. Researchers are urgently developing antibody-based kits for SARS-CoV-2 detection and antibody drugs for COVID-19 treatment. The spike protein of SARS-CoV-2, which is crucial for viral infection, has been extensively studied and its receptor-binding domain (RBD) has become a major target for therapeutic antibody development. Given the high mutation rate of SARS-CoV-2, especially under the pressure of prophylactic vaccines and neutralizing antibodies, the use of antibody cocktails is expected to be an important strategy for effective COVID-19 treatment. Additionally, antibodies against cytokine storms, which can be triggered by SARS-CoV-2 infection and drive severe disease progression, are also being developed as treatments for COVID-19. In addition to their use as drugs, antibodies are currently being used in SARS-CoV-2 detection tests, including antigen and immunoglobulin tests, which are crucial surveillance tools for preventing the spread of COVID-19.

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Bi-paratopic and multivalent VH domains block ACE2 binding and neutralize SARS-CoV-2

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Summary: This study presents a strategy to rapidly identify and assemble synthetic human VH domains for neutralizing SARS-CoV-2, which was proven to be effective through experimental validation.

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Summary: This study explores the development of ACE2-IgG4-Fc fusion proteins for neutralizing SARS-CoV-2 variants without activating Fc receptors, maintaining the enzymatic activity of ACE2. These promising fusion proteins show potential as candidate antivirals to combat current and future pandemics.

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Prospective mapping of viral mutations that escape antibodies used to treat COVID-19

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Conformational dynamics of SARS-CoV-2 trimeric spike glycoprotein in complex with receptor ACE2 revealed by cryo-EM

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Summary: The recent global health emergency caused by SARS-CoV-2 outbreak is mediated by the interaction between the SARS-CoV-2 trimeric spike glycoprotein and the human ACE2 receptor. The SARS-CoV-2 S trimer is more sensitive to ACE2 receptor compared to SARS-CoV S trimer, potentially contributing to its superior infectivity. Research findings depict the mechanism of ACE2-induced conformational transitions in S trimer structure, aiding in the development of anti-SARS-CoV-2 vaccines and therapeutics.

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Resistance of SARS-CoV-2 variants to neutralization by monoclonal and serum-derived polyclonal antibodies

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Summary: The study analyzed antibody neutralization activity against a panel of authentic isolates and chimeric SARS-CoV-2 variants, showing significantly reduced neutralizing activity against the B.1.351 variant first identified in South Africa. Antibodies targeting the receptor-binding domain and N-terminal domain, monoclonal antibodies, convalescent sera, and mRNA vaccine-induced immune sera exhibited decreased inhibitory activity against viruses with an E484K spike mutation, suggesting a need for updated monoclonal antibodies or vaccine adjustments to prevent loss of protection against emerging variants.

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Summary: COVID-19 is a severe acute respiratory disease caused by SARS-CoV-2, which utilizes human ACE2 enzyme as receptor for cell entry. Researchers have used phage display to select anti-SARS-CoV-2 spike antibodies from universal antibody gene libraries, showing potential inhibition of infection.

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Summary: The interaction between the Spike protein of SARS-CoV-2 and ACE2 on host cells is crucial for viral entry, with glycosylation playing a critical role. Engineering ACE2 glycosylation can enhance virus neutralization without affecting protein stability or activity. Removing all N-glycans from recombinant soluble human ACE2 can create a superior decoy receptor for effective COVID-19 treatment.

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His345 mutant of angiotensin-converting enzyme 2 (ACE2) remains enzymatically active against angiotensin II

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Dual nature of human ACE2 glycosylation in binding to SARS-CoV-2 spike

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CANADIAN JOURNAL OF PHYSIOLOGY AND PHARMACOLOGY (2002)

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Review Immunology

IgG4 breaking the rules

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IMMUNOLOGY (2002)

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Article Immunology

Recombinant CD4-IgG2 in human immunodeficiency virus type 1-infected children: Phase 1/2 study

WT Shearer et al.

JOURNAL OF INFECTIOUS DISEASES (2000)

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Article Cardiac & Cardiovascular Systems

A novel angiotensin-converting enzyme-related carboxypeptidase (ACE2) converts angiotensin I to angiotensin 1-9

M Donoghue et al.

CIRCULATION RESEARCH (2000)

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Article Nutrition & Dietetics

Function and mechanism of zinc metalloenzymes

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JOURNAL OF NUTRITION (2000)

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