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Your search keyword '"Sastry, Mallika"' showing total 2 results
Start Over Author "Sastry, Mallika" Publisher american association for the advancement of science
2 results on '"Sastry, Mallika"'

1. Prefusion F–specific antibodies determine the magnitude of RSV neutralizing activity in human sera.

Author

Ngwuta, Joan O., Chen, Man, Modjarrad, Kayvon, Joyce, M. Gordon, Masaru Kanekiyo, Kumar, Azad, Yassine, Hadi M., Moin, Syed M., Killikelly, April M., Gwo-Yu Chuang, Druz, Aliaksandr, Georgiev, Ivelin S., Rundlet, Emily J., Sastry, Mallika, Stewart-Jones, Guillaume B. E., Yongping Yang, Zhang, Baoshan, Nason, Martha C., Capella, Cristina, and Peeples, Mark E.

Subjects
RESPIRATORY syncytial virus, SERUM, MUTANT proteins, MONOCLONAL antibodies, VACCINATION
Abstract

The article presents research conducted by Joan O. Ngwuta on the activity of perfusion F-specific antibodies in determining the magnitude of Respiratory syncytial virus (RSV) neutralizing activity in human sera. Topics discussed include protein competition assays with perfusion F mutants to knock out binding corresponding sites; detection of site-specific antibodies by competition assays with monoclonal antibodies; and boosting of neutralizing activity by vaccination.

Published
2015
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2. Structure-Based Design of a Fusion Glycoprotein Vaccine for Respiratory Syncytial Virus.

Author

McLellan, Jason S., Chen, Man, Joyce, M. Gordon, Sastry, Mallika, Stewart-Jones, Guillaume B. E., Yongping Yang, Baoshan Zhang, Lei Chen, Srivatsan, Sanjay, Anqi Zheng, Tongqing Zhou, Graepel, Kevin W., Kumar, Azad, Moin, Syed, Boyington, Jeffrey C., Gwo-Yu Chuang, Soto, Cinque, Baxa, Ulrich, Bakker, Arjen Q., and Spits, Hergen

Subjects
*RESPIRATORY syncytial virus infection vaccines, *VIRAL antigen biotechnology, *VACCINE biotechnology, *GLYCOPROTEINS, *RECOMBINANT fusion proteins, *PROTEIN crystallography
Abstract

Respiratory syncytial virus (RSV) is the leading cause of hospitalization for children under 5 years of age. We sought to engineer a viral antigen that provides greater protection than currently available vaccines and focused on antigenic site Ø, a metastable site specific to the prefusion state of the RSV fusion (F) glycoprotein, as this site is targeted by extremely potent RSV-neutralizing antibodies. Structure-based design yielded stabilized versions of RSV F that maintained antigenic site Ø when exposed to extremes of pH, osmolality, and temperature. Six RSV F crystal structures provided atomic-level data on how introduced cysteine residues and filled hydrophobic cavities improved stability. Immunization with site Ø--stabilized variants of RSV F in mice and macaques elicited levels of RSV-specific neutralizing activity many times the protective threshold. [ABSTRACT FROM AUTHOR]

Published
2013
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