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Discovery of Neutralizing Antibody (NAb) and Peptide Targeting Ebola Virus

Discovery of Neutralizing Antibody (NAb) and Peptide Targeting Ebola Virus

Neutralizing antibodies can be useful in vaccine design and as a prophylactic agent against Ebola virus infection. Creative Biolabs has established an advanced AntInfectâ„¢ Platform for anti-infectives biomolecular discovery. Equipped with enriched experience, profound expertise and state-of-the-art instruments, Creative Biolabs offers high-quality Ebola virus NAbs and functional peptides discovery services for our global customers.

Overview of Ebola Virus Disease

Ebola virus was first discovered in 1976 near the Ebola River. Since then, the virus has been infecting people from time to time, leading to outbreaks in several African countries. Ebola virus disease is a rare and deadly disease most commonly affecting people and nonhuman primates (monkeys, gorillas, and chimpanzees). Symptoms of Ebola virus diseases include abrupt fever, headache, joint pain, muscle aches, sore throat, and weakness. Progression of Ebola symptoms includes diarrhea, vomiting, stomach pain, hiccups, rash, and internal and external bleeding in many patients. Ebola hemorrhagic fever is a disease caused by four different strains of Ebola virus. Compared to most illnesses, Ebola hemorrhagic fever has a relatively short history.

Targets for Neutralization of Ebola Virus

Discovery of Neutralizing Antibody (NAb) and Peptide Targeting Ebola Virus

The Ebola virus envelope contains a single surface protein, glycoprotein (GP), which forms a trimer. The GP protomer consists of two subunits, GP1 and GP2. The GP1 subunit has a heavily glycosylated mucin-like domain and a glycan cap, which shields the host receptor binding site (RBS) that binds to domain C of its endosomal receptor, the protein Niemann-Pick C1 (NPC1-C). The GP2 subunit contains the internal fusion loop (IFL) and stalk and is anchored into the viral membrane by a transmembrane domain. The GP is solely responsible for viral attachment to the host cell, endosomal entry, and membrane fusion, and thus it is the major target for NAbs and vaccine design.

The Clinical Importance for the Development of NAb and Peptide Targeting Ebola Virus

There is no standard treatment for Ebola hemorrhagic fever; only supportive therapy and experimental treatment are available. There are many complications from Ebola hemorrhagic fever causing a high mortality rate (25%-100%). Researchers are trying to understand the Ebola virus and pinpoint its ecological reservoirs to deduce how Ebola outbreaks occur, and are actively trying to develop an effective vaccine against Ebola viruses. Identification of neutralizing antibodies that are effective against multiple ebolaviruses are urgently for therapeutics development. Peptides can be good therapeutics as they are generally selective and safe and well tolerated. Researchers have identified natural and unnatural peptides that bind Ebola virus glycoproteins. The positive peptide hits could form the basis of new Ebola therapies.

Discovery Service of NAb and Peptide Targeting Ebola Virus in Creative Biolabs

Ebola virus NAbs are promising candidates for development as broadly protective pan-ebolavirus therapeutic molecules. Creative Biolabs is one of the well-recognized experts who are professional in NAbs for a broad range of project objectives. We are pleased to use our extensive experience and advanced Anti-Virus Biomolecular Discovery system to offer the best service of Ebola virus NAbs development to satisfy each demand from our customers.

We offer turn-key or ala carte services customized to our client’s needs. Please contact us for more information and a detailed quote.

References:

  1. Flyak, A.I.; et al. Broadly neutralizing antibodies from human survivors target a conserved site in the Ebola virus glycoprotein HR2-MPER region. Nat Microbiol. 2018, 3(6):670-677.
  2. Gilchuk, P.; et al. Multifunctional pan-ebolavirus antibody recognizes a site of broad vulnerability on the Ebolavirus glycoprotein. Immunity. 2018, 49(2):363-374.e10.
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