Title Information
Title
IDENTIFICATION AND FUNCTIONAL CHARACTERIZATION OF P113 AS A NOVEL BLOOD-STAGE VACCINE TARGET AGAINST SEVERE PLASMODIUM FALCIPARUM MALARIA
Type of Resource (primo)
dissertations
Name: Personal
Name Part
Zheng, Yiyu
Role
Role Term: Text
creator
Name: Personal
Name Part
Kurtis, Jonathan D.
Role
Role Term: Text
Advisor
Name: Personal
Name Part
Wu, Hannah Wei
Role
Role Term: Text
Reader
Name: Personal
Name Part
Najrana, Tanbir
Role
Role Term: Text
Reader
Name: Corporate
Name Part
Brown University. Biology and Medicine: Biotechnology
Role
Role Term: Text
sponsor
Origin Information
Copyright Date
2026
Physical Description
Extent
vii, 50 p.
digitalOrigin
born digital
Note: thesis
Thesis (Sc. M.)--Brown University, 2026
Genre (aat)
theses
Abstract
Malaria is a leading cause of child mortality worldwide and a significant burden on global health. The severe malaria (SM) subtype is particularly consequential, carrying a case fatality rate of 20%. Although pre-erythrocytic vaccines such as RTS,S/AS01 and R21/Matrix-M have been approved for malaria prevention, they are limited in targeting SM cases, as their efficacy diminishes over time due to parasite resistance, and neither targets blood-stage parasites directly, which are especially responsible for SM pathology. Previous studies have shown that naturally acquired immunity to SM develops rapidly, usually after only one or two episodes. Since this immunity is mediated primarily by antibodies, this study aimed to identify the specific parasite antigens targeted by these protective responses. In this thesis, we performed whole-proteome differential screening (WPDS) using post-SM plasma from our Kenyan cohort and a Plasmodium falciparum 3D7 cDNA library displayed in T7 phage, leading to the identification of 46 parasite proteins uniquely recognized by antibodies from children with severe malaria. Among these candidates, we prioritized PfP113 (P113; PF3D7_1420700) based on its enrichment, biochemical features, and biological relevance. P113 is a 112.6-kDa GPI-anchored merozoite surface protein which anchors the PfRh5 invasion complex to the merozoite surface and displays limited sequence variation across field isolates, making it an attractive vaccine candidate. PfGARP is a previously validated vaccine target from the Kurtis Laboratory, was independently recovered in the screen (34.4% of fourth-round clones) and was utilized as an internal positive control. Recombinant P113 was expressed in Expi293F cells, purified by nickel-column immobilized metal affinity chromatography, and validated by LC-MS/MS mass spectrometry. Mice (BALB/c) immunized with recombinant P113 formulated with TiterMax Gold adjuvant developed anti-P113 antibodies. However, only ~20% of immunized mice (out of 45 mice, with initial cohort of 5 showing 1 responder) produced sera with growth-inhibitory activity against P. falciparum 3D7 parasites in vitro, as measured by growth inhibition assay. Comparison of inhibitory and non-inhibitory sera indicated that both groups had comparable antibody titers and both recognized native P113 in parasite lysates by Western blot. This demonstrates that the growth-inhibitory phenotype is not determined by antibody quantity or overall antigen recognition. Epitope mapping revealed that inhibitory and non-inhibitory sera shared broadly similar binding profiles, yet the inhibitory sera uniquely recognized a shifted epitope, HLQGSEQSIEASESS, which suggests that antibodies targeting this specific region may be responsible for functional parasite growth inhibition. Collectively, these findings advance P113 from a bioinformatically identified candidate to a functionally validated blood-stage vaccine antigen. This study also provides the first evidence that immunization-induced anti-P113 antibodies can inhibit P. falciparum growth. The identification of a candidate inhibitory epitope establishes a foundation for focused peptide–conjugate immunization strategies aimed at improving the responder rate. This work contributes to the expanding repertoire of blood-stage antigens targeting severe P. falciparum malaria and supports the development of P113 as a component of a multi-antigen vaccine strategy.
Subject (fast) (authorityURI="http://id.worldcat.org/fast", valueURI="http://id.worldcat.org/fast/01019337")
Topic
Mice
Subject (fast) (authorityURI="http://id.worldcat.org/fast", valueURI="http://id.worldcat.org/fast/01163573")
Topic
Vaccines
Subject (fast) (authorityURI="http://id.worldcat.org/fast", valueURI="http://id.worldcat.org/fast/01006371")
Topic
Malaria vaccine
Subject (fast) (authorityURI="http://id.worldcat.org/fast", valueURI="http://id.worldcat.org/fast/01154588")
Topic
Transfection
Subject (fast) (authorityURI="http://id.worldcat.org/fast", valueURI="http://id.worldcat.org/fast/01066401")
Topic
Plasmodium falciparum
Subject
Topic
severe malaria
Subject
Topic
Antibody
Subject
Topic
P113 Protein
Subject
Topic
whole proteome differential screening (WPDS)
Subject
Topic
Vaccine antigen discovery
Subject
Topic
Epitope mapping
Subject
Topic
Growth inhibition assay
Subject (fast) (authorityURI="http://id.worldcat.org/fast", valueURI="http://id.worldcat.org/fast/02021255")
Topic
Merozoite surface proteins
Subject
Topic
Protective immunity
Language
Language Term (ISO639-2B)
English
Record Information
Record Content Source (marcorg)
RPB
Record Creation Date (encoding="iso8601")
20260516