Author Type

Graduate Student

Date of Award

Spring 4-9-2026

Document Type

Thesis

Publication Status

Version of Record

Submission Date

April 2026

Department

Biomedical Science

College Granting Degree

Charles E. Schmidt College of Medicine

Department Granting Degree

Biomedical Sciences

Degree Name

Master of Science (MS)

Thesis/Dissertation Advisor [Chair]

Andrew Oleinikov

Abstract

Host-pathogen protein-protein interactions are the key drivers of infectious diseases, where events such as pathogen adhesion and signaling are directly associated with disease severity. One example of this is Malaria, in which the Plasmodium falciparum infected erythrocytes adhere to endothelial receptors to avoid splenic clearance. This study investigated interactions between PfEMP1 CIDR1 field domains and host receptor CD36 using a multiplex platform to quantitatively determine binding affinities. Variants RP18 and RP27 exhibited strong affinity, suggesting a role in cytoadherence and disease severity. To evaluate broader applicability, the platform was expanded to the interaction between host protein SIVA1 and Helicobacter pylori effector protein CagA. A pilot small-molecule screen further demonstrated feasibility for identifying inhibitors of this protein-protein interaction. The results obtained establish Bio-Plex as a versatile tool for quantifying host-pathogen interactions and supporting development of anti-adhesion therapeutic strategies.

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