The Marburgvirus-Neutralizing Human Monoclonal Antibody MR191 Targets a Conserved Site to Block Virus Receptor Binding

doi:10.1016/j.chom.2017.12.003

Title: The Marburgvirus-Neutralizing Human Monoclonal Antibody MR191 Targets a Conserved Site to Block Virus Receptor Binding

Full Record
Other Related Research

Authors:: King, Liam B.; Fusco, Marnie L.; Flyak, Andrew I.; Ilinykh, Philipp A.; Huang, Kai; Gunn, Bronwyn; Kirchdoerfer, Robert N.; Hastie, Kathryn M.; Sangha, Amandeep K.; Meiler, Jens; Alter, Galit; Bukreyev, Alexander; Crowe, Jr., James E.; Saphire, Erica Ollmann

Publication Date:: 2018-01-01

Sponsoring Org.:: USDOE Office of Science (SC), Basic Energy Sciences (BES); USDOE Office of Science (SC), Biological and Environmental Research (BER)

OSTI Identifier:: 1548820

Grant/Contract Number:: AC02-06CH11357; AC02-76SF00515

Resource Type:: Published Article

Journal Name:: Cell Host & Microbe

Additional Journal Information:: Journal Name: Cell Host & Microbe Journal Volume: 23 Journal Issue: 1; Journal ID: ISSN 1931-3128

Publisher:: Elsevier

Country of Publication:: Netherlands

Language:: English

Citation Formats


                    King, Liam B., Fusco, Marnie L., Flyak, Andrew I., Ilinykh, Philipp A., Huang, Kai, Gunn, Bronwyn, Kirchdoerfer, Robert N., Hastie, Kathryn M., Sangha, Amandeep K., Meiler, Jens, Alter, Galit, Bukreyev, Alexander, Crowe, Jr., James E., and Saphire, Erica Ollmann. The Marburgvirus-Neutralizing Human Monoclonal Antibody MR191 Targets a Conserved Site to Block Virus Receptor Binding.  Netherlands: N. p., 2018. 
        Web.  doi:10.1016/j.chom.2017.12.003.

Copy to clipboard


                    King, Liam B., Fusco, Marnie L., Flyak, Andrew I., Ilinykh, Philipp A., Huang, Kai, Gunn, Bronwyn, Kirchdoerfer, Robert N., Hastie, Kathryn M., Sangha, Amandeep K., Meiler, Jens, Alter, Galit, Bukreyev, Alexander, Crowe, Jr., James E., & Saphire, Erica Ollmann. The Marburgvirus-Neutralizing Human Monoclonal Antibody MR191 Targets a Conserved Site to Block Virus Receptor Binding.  Netherlands.  doi:10.1016/j.chom.2017.12.003.

Copy to clipboard


                    King, Liam B., Fusco, Marnie L., Flyak, Andrew I., Ilinykh, Philipp A., Huang, Kai, Gunn, Bronwyn, Kirchdoerfer, Robert N., Hastie, Kathryn M., Sangha, Amandeep K., Meiler, Jens, Alter, Galit, Bukreyev, Alexander, Crowe, Jr., James E., and Saphire, Erica Ollmann. Mon .  
        "The Marburgvirus-Neutralizing Human Monoclonal Antibody MR191 Targets a Conserved Site to Block Virus Receptor Binding".  Netherlands.  doi:10.1016/j.chom.2017.12.003.

Copy to clipboard


                    
@article{osti_1548820,

  title        = {The Marburgvirus-Neutralizing Human Monoclonal Antibody MR191 Targets a Conserved Site to Block Virus Receptor Binding},

  author       = {King, Liam B. and Fusco, Marnie L. and Flyak, Andrew I. and Ilinykh, Philipp A. and Huang, Kai and Gunn, Bronwyn and Kirchdoerfer, Robert N. and Hastie, Kathryn M. and Sangha, Amandeep K. and Meiler, Jens and Alter, Galit and Bukreyev, Alexander and Crowe, Jr., James E. and Saphire, Erica Ollmann},

  abstractNote = {},

  doi          = {10.1016/j.chom.2017.12.003},

  journal      = {Cell Host & Microbe},

  number       = 1,

  volume       = 23,

  place        = {Netherlands},

  year         = {2018},

  month        = {1}

}

Copy to clipboard

Journal Article:

Free Publicly Available Full Text

Publisher's Version of Record
DOI: 10.1016/j.chom.2017.12.003

Other availability

Search WorldCat to find libraries that may hold this journal

Citation Metrics:

Cited by: 9 works

Citation information provided by
Web of Science

Save / Share:

Export Metadata

Save to My Library

Similar Records in DOE PAGES and OSTI.GOV collections:

The Marburgvirus-Neutralizing Human Monoclonal Antibody MR191 Targets a Conserved Site to Block Virus Receptor Binding

Journal Article King, Liam B. ; Fusco, Marnie L. ; Flyak, Andrew I. ; ... - Cell Host & Microbe
DOI: 10.1016/j.chom.2017.12.003
IL-12: Monoclonal antibodies specific for the 40-kDa subunit block receptor binding and biologic activity on activated human lymphoblasts

Journal Article Chizzonite, R ; Truitt, T ; Podlaski, F J ; ... - Journal of Immunology; (United States)

IL-12, formerly known as cytotoxic lymphocyte maturation factor, is a cytokine that stimulates proliferation of PHA-activated human peripheral blood lymphoblasts and synergizes with low concentrations of IL-2 in the induction of lymphokine-activated killer cells. IL-12 is a 75-kDa heterodimer composed of disulfide-bonded 40-kDa and 35-kDa subunits. mAb prepared against a partially purified preparation of natural IL-12 have been characterized by (1) immunoprecipitation of 125I-labeled IL-12, (2) immunodepletion of IL-12 bioactivity, (3) Western blotting of IL-12, (4) inhibition of (125I)IL-12 binding to its cellular receptor, and (5) neutralization of IL-12 bioactivity. Twenty antibodies immunoprecipitate 125I-labeled IL-12 and immunodeplete IL-12 bioactivity asmore »« less
Cross-reactive neutralizing human survivor monoclonal antibody BDBV223 targets the ebolavirus stalk

Journal Article King, Liam B. ; West, Brandyn R. ; Moyer, Crystal L. ; ... - Nature Communications

Three Ebolavirus genus viruses cause lethal disease and lack targeted therapeutics: Ebola virus, Sudan virus and Bundibugyo virus. Monoclonal antibody (mAb) cocktails against the surface glycoprotein (GP) present a potential therapeutic strategy. Here we report two crystal structures of the antibody BDBV223, alone and complexed with its GP2 stalk epitope, an interesting site for therapeutic/vaccine design due to its high sequence conservation among ebolaviruses. BDBV223, identified in a human survivor of Bundibugyo virus disease, neutralizes both Bundibugyo virus and Ebola virus, but not Sudan virus. Importantly, the structure suggests that BDBV223 binding interferes with both the trimeric bundle assembly ofmore »« less
DOI: 10.1038/s41467-019-09732-7

Full Text Available
Structural analysis of a novel rabbit monoclonal antibody R53 targeting an epitope in HIV-1 gp120 C4 region critical for receptor and co-receptor binding

Journal Article Pan, Ruimin ; Chen, Yuxin ; Vaine, Michael ; ... - Emerging Microbes & Infections

The fourth conserved region (C4) in the HIV-1 envelope glycoprotein (Env) gp120 is a structural element that is important for its function, as it binds to both the receptor CD4 and the co-receptor CCR5/CXCR4. It has long been known that this region is highly immunogenic and that it harbors B-cell as well as T-cell epitopes. It is the target of a number of antibodies in animal studies, which are called CD4-blockers. However, the mechanism by which the virus shields itself from such antibody responses is not known. Here, we determined the crystal structure of R53 in complex with its epitopemore »« less
Cited by 5
DOI: 10.1038/emi.2015.44

Full Text Available
A multifunctional human monoclonal neutralizing antibody that targets a unique conserved epitope on influenza HA

Journal Article Bangaru, Sandhya ; Zhang, Heng ; Gilchuk, Iuliia M. ; ... - Nature Communications
DOI: 10.1038/s41467-018-04704-9

Similar Records