자료유형  

 학위논문

Control Number  

0016932548

International Standard Book Number  

9798379680671

Dewey Decimal Classification Number  

600

Main Entry-Personal Name  

Fu, Jianing.

Publication, Distribution, etc. (Imprint  

[S.l.] : Purdue University., 2020

Publication, Distribution, etc. (Imprint  

Ann Arbor : ProQuest Dissertations & Theses, 2020

Physical Description  

1 online resource(100 p.)

General Note  

Source: Dissertations Abstracts International, Volume: 84-12, Section: A.

General Note  

Advisor: Kuhn, Richard J.

Dissertation Note  

Thesis (Ph.D.)--Purdue University, 2020.

Restrictions on Access Note  

This item must not be sold to any third party vendors.

Summary, Etc.  

요약Enterovirus (EV), a genus within the Picornaviridae family, contains icosahedral positivestranded RNA viruses linked to different human and mammalian diseases with a variety of symptoms ranging from the common cold to central nervous system infection. An important member within this genus is EV-D68. Unlike many enteroviruses that use the gastrointestinal tract as the transmission and propagation route, EV-D68 infects the respiratory tract and causes respiratory illness, especially in children. Severe infections of EV-D68 also lead to acute flaccid myelitis (AFM), a polio-like neurological disease. Especially in recent years, EV-D68 has been on a global upswing. However, no antiviral interventions against EV-D68 infection have been developed to date. Antibodies neutralizing EV-D68 have significant vaccine and therapeutic potentials. Here, the structures of the immune complex between EV-D68 and the Fab molecules of EV-D68 human monoclonal antibodies have been reconstructed using cryo-electron microscopy (cryo-EM). These structures show two Fab binding loci on the virion surface as well as the essential amino acids involved in binding. In addition to antibodies, a drug candidate against EVD68 has been investigated in this work as an antiviral strategy. It is likely that this drug blocks viral entry through binding in the hydrophobic pocket underneath the viral protein 1, the largest structural protein of EV-D68. Furthermore, the morphogenesis of EV-D94, another causative virus of polio-like disease, which is closely related to EV-D68 with 85% sequence identity, has been investigated using cryo-EM. Compared to EV-D68, the shape of the canyon and the loops containing the immunogenic recognition sites are different in EV-D94. The structures of each of the three stages of EV-D94 particles (the full native virion, the uncoating intermediate, and the empty virion) were identified and delineate the viral uncoating process. These findings reveal useful knowledge and new insights to develop treatments against human EVs.

Subject Added Entry-Topical Term  

Infections.

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Monoclonal antibodies.

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Propagation.

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Young adults.

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Encephalitis.

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Hydrogen bonds.

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Epidemics.

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Microscopy.

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Labeling.

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Maps.

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Cardiomyopathy.

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Families & family life.

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Foot & mouth disease.

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Meningitis.

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Amino acids.

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Viruses.

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Genomes.

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Nervous system.

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Poliomyelitis.

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Respiratory diseases.

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Atoms & subatomic particles.

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Crystallography.

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Animal diseases.

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Atomic physics.

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Epidemiology.

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Genetics.

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Individual & family studies.

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Medicine.

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Neurosciences.

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Physics.

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Virology.

Added Entry-Corporate Name  

Purdue University.

Host Item Entry  

Dissertations Abstracts International. 84-12A.

Host Item Entry  

Dissertation Abstract International

Electronic Location and Access  

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Control Number  

joongbu:641377