AI Article Synopsis

  • Fourteen P. falciparum proteins were evaluated for their potential as vaccine candidates targeting pre-erythrocytic stages, focusing on those involved in sporozoite infection of liver cells.
  • Chimeric P. berghei sporozoites were engineered to express these P. falciparum proteins, but only six out of fourteen were found to induce a protective immune response in mice after vaccination and subsequent exposure to the chimeric parasites.
  • Among the six proteins tested, only SPELD showed partial protection, highlighting both the challenges in eliciting strong immune responses and the detrimental effects of some P. falciparum proteins on sporozoite infectivity.

Article Abstract

To screen for additional vaccine candidate antigens of Plasmodium pre-erythrocytic stages, fourteen P. falciparum proteins were selected based on expression in sporozoites or their role in establishment of hepatocyte infection. For preclinical evaluation of immunogenicity of these proteins in mice, chimeric P. berghei sporozoites were created that express the P. falciparum proteins in sporozoites as an additional copy gene under control of the uis4 gene promoter. All fourteen chimeric parasites produced sporozoites but sporozoites of eight lines failed to establish a liver infection, indicating a negative impact of these P. falciparum proteins on sporozoite infectivity. Immunogenicity of the other six proteins (SPELD, ETRAMP10.3, SIAP2, SPATR, HT, RPL3) was analyzed by immunization of inbred BALB/c and outbred CD-1 mice with viral-vectored (ChAd63 or ChAdOx1, MVA) vaccines, followed by challenge with chimeric sporozoites. Protective immunogenicity was determined by analyzing parasite liver load and prepatent period of blood stage infection after challenge. Of the six proteins only SPELD immunized mice showed partial protection. We discuss both the low protective immunogenicity of these proteins in the chimeric rodent malaria challenge model and the negative effect on P. berghei sporozoite infectivity of several P. falciparum proteins expressed in the chimeric sporozoites.

Download full-text PDF

Source
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC8274855PMC
http://journals.plos.org/plosone/article?id=10.1371/journal.pone.0254498PLOS

Publication Analysis

Top Keywords

falciparum proteins
16
immunogenicity proteins
12
chimeric rodent
8
proteins
8
sporozoite infectivity
8
proteins speld
8
chimeric sporozoites
8
protective immunogenicity
8
sporozoites
7
chimeric
6

Similar Publications

Plasmodium falciparum erythrocyte membrane protein 1 (PfEMP1) is a diverse family of variant surface antigens, encoded by var genes, that mediates binding of infected erythrocytes to human cells and plays a key role in parasite immune evasion and malaria pathology. The increased availability of parasite genome sequence data has revolutionised the study of PfEMP1 diversity across multiple P. falciparum isolates.

View Article and Find Full Text PDF

Biolayer interferometry (BLI) is an optical sensor-based analytical method primarily used for analyzing interactions between biomolecules. In this study, we explored the application of BLI to observe the cleavage reaction of glutathione S-transferase (GST)-tagged fusion protein by human rhinovirus (HRV) 3C protease on a BLI sensor as a new application of the BLI method. The soluble domain of the Tic22 protein from was expressed and purified as a GST-tagged fusion protein, GST-Tic22, in .

View Article and Find Full Text PDF

mosGILT antibodies interfere with Plasmodium sporogony in Anopheles gambiae.

Nat Commun

January 2025

Section of Infectious Diseases, Department of Internal Medicine, Yale University School of Medicine, New Haven, CT, 06520, USA.

Plasmodium, the causative agents of malaria, are obtained by mosquitoes from an infected human. Following Plasmodium acquisition by Anopheles gambiae, mosquito gamma-interferon-inducible lysosomal thiol reductase (mosGILT) plays a critical role in its subsequent sporogony in the mosquito. A critical location for this development is the midgut, a tissue we show expresses mosGILT.

View Article and Find Full Text PDF

It is established that reverse hydroxamate analogs of fosmidomycin inhibit the growth of by inhibiting 1-deoxy-d-xylulose 5-phosphate reductoisomerase (DXR), the second enzyme of the non-mevalonate pathway, which is absent in humans. Recent biochemical studies have demonstrated that novel reverse fosmidomycin analogs with phenylalkyl substituents at the hydroxamate nitrogen exhibit inhibitory activities against DXR at the nanomolar level. Moreover, crystallographic analyses have revealed that the phenyl moiety of the -phenylpropyl substituent is accommodated in a previously unidentified subpocket within the active site of DXR.

View Article and Find Full Text PDF

Want AI Summaries of new PubMed Abstracts delivered to your In-box?

Enter search terms and have AI summaries delivered each week - change queries or unsubscribe any time!