Siglec homologs interact with membrane-bound Heat Shock Protein 70 (Hsp70) during early infection of the Schistosoma mansoni susceptible (BB02) Biomphalaria glabrata snail host

Authors

Eli Vanlal, Division of Science & Mathematics, University of the District of Columbia, 4200 Connecticut Ave. NW, Washington, DC, 20008, USA.
Oumsalama Elhelu, Division of Science & Mathematics, University of the District of Columbia, 4200 Connecticut Ave. NW, Washington, DC, 20008, USA; Howard University, 2400 Sixth St NW, Washington, DC, 20059, USA.
Olayemi G. Fagunloye, Division of Science & Mathematics, University of the District of Columbia, 4200 Connecticut Ave. NW, Washington, DC, 20008, USA.
Matty Knight, Division of Science & Mathematics, University of the District of Columbia, 4200 Connecticut Ave. NW, Washington, DC, 20008, USA; Department of Microbiology, Immunology & Tropical Medicine, Research Center for Neglected Diseases of Poverty, School of Medicine & Health Sciences, The George Washington University, Ross Hall, 2300 I Street, NW, Washington, DC, 20037, USA. Electronic address: mathilde.knight@udc.edu.

Document Type

Journal Article

Publication Date

10-27-2025

Journal

Experimental parasitology

DOI

10.1016/j.exppara.2025.109042

Keywords

Biomphalaria glabrata; Homology; Innate immunity; Schistosoma mansoni; Schistosomiasis; Siglec

Abstract

Sialic acid-binding immunoglobulin-like lectins (siglecs) are cell surface receptors involved in immune signaling. When Schistosoma mansoni infects its intermediate host, the Biomphalaria glabrata snail, early stress responses such as upregulation of heat shock protein 70 (Hsp70) are observed. We hypothesized that stress-induced Hsp70 translocates to the cell membrane and interacts with siglec homologs to modulate immune response in the snail. Utilizing in-silico approaches, we identified B. glabrata transcripts homologous to human and molluscan siglecs, followed by homology modeling and molecular docking, which predicted a salt bridge between glutamic acid 479 on Hsp70 and lysine 47 on a siglec homolog, (BgPrx), suggesting a plausible binding interface. To validate this, we performed real-time qPCR from infected BB02 snails, revealing significant upregulation of siglec homolog transcripts shortly after infection. Additionally, protein fractionation and immunocytochemistry confirmed Hsp70 localization to the membrane post infection. These results support a model in which siglec-Hsp70 interactions dampen stress signaling and may suppress host immune defenses. Concurrently, S. mansoni employs glycan mimicry, presenting host-like sialylated structures that likely engage siglecs and further misdirect the immune response. Together, our findings suggest that BgHsp70-siglec interactions, in combination with parasite glycan mimicry, constitute a potential immune evasion mechanism enabling schistosome establishment in susceptible B. glabrata snails.

APA Citation

Vanlal, Eli; Elhelu, Oumsalama; Fagunloye, Olayemi G.; and Knight, Matty, "Siglec homologs interact with membrane-bound Heat Shock Protein 70 (Hsp70) during early infection of the Schistosoma mansoni susceptible (BB02) Biomphalaria glabrata snail host" (2025). GW Authored Works. Paper 8222.
https://hsrc.himmelfarb.gwu.edu/gwhpubs/8222

Department

Microbiology, Immunology, and Tropical Medicine