Identification of the glycan binding profile of human and rodent Plasmodium sporozoites

Poole, Jessica, Hartley-Tassell, Lauren E., Day, Christopher J., Stanisic, Danielle I., Groves, Penny L., Chakravarty, Sumana, Lee Sim, B. Kim, Hoffman, Stephen L., Tiralongo, Joe, Bovin, Nicolai, Doolan, Denise L., and Jennings, Michael P. (2021) Identification of the glycan binding profile of human and rodent Plasmodium sporozoites. ACS Infectious Diseases, 7 (8). pp. 2383-2389.

[img] PDF (Published Version) - Published Version
Restricted to Repository staff only

View at Publisher Website:


The transmission of Plasmodium spp. sporozoites to the mammalian host is the first step in the initiation of the mosquito-borne disease known as malaria. The exact route of transmission from the bloodstream to the liver is still not clearly elucidated, and identification of the host glycan structures bound by the sporozoites may inform as to which host cells are involved. Here, we provide a comprehensive analysis of the glycan structures that sporozoites from the human pathogen, P. falciparum, and the rodent pathogen, P. yoelii, recognize and bind. Glycan array analysis was used to profile the glycans bound by the sporozoites, and the binding affinities of these sporozoite-glycan interactions were then determined by surface plasmon resonance. Data showed that the different Plasmodium spp. bind different classes of glycans. P. falciparum was observed to bind to glycans with terminal N-acetylgalactosamine (GalNAc) or Galactose (Gal) linked to a GalNAc, and the highest-affinity observed was with the GalNAc monosaccharide (12.5 nM). P. yoelii bound glycosaminoglycans, mannosyl glycans, Gal linked to N-acetylglucosamine structures, and the αGal epitope. The highest-affinity interaction for P. yoelii was with the αGal epitope (31.4 nM). This is the first study to identify the key host glycan structures recognized by human and rodent Plasmodium spp. sporozoites. An understanding of how Plasmodium sporozoites interact with the specific glycan structures identified here may provide further insight into this infectious disease that could help direct the design of an effective therapeutic.

Item ID: 72693
Item Type: Article (Research - C1)
ISSN: 2373-8227
Copyright Information: © 2021 American Chemical Society
Funders: National Health and Medical Research Council (NHMRC)
Projects and Grants: NHMRC #1037304, NHMRC #1071659, NHMRC #1023636, NHMRC #1138466
Date Deposited: 01 Mar 2022 01:51
FoR Codes: 32 BIOMEDICAL AND CLINICAL SCIENCES > 3207 Medical microbiology > 320704 Medical parasitology @ 100%
SEO Codes: 20 HEALTH > 2001 Clinical health > 200104 Prevention of human diseases and conditions @ 100%
Downloads: Total: 1
More Statistics

Actions (Repository Staff Only)

Item Control Page Item Control Page