Yagya D. Sharma

New Delhi, DL, India

Last Updated: 09/26/2026

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Found 21 publications

Majority of the erythrocyte binding proteins of the Pvfam "a" family of Plasmodium vivax interact with Basigin to assist parasite entry into the host cell.

Majority of the erythrocyte binding proteins of the Pvfam "a" family of Plasmodium vivax interact with Basigin to assist parasite entry into the host cell.

Journal: Frontiers in cellular and infection microbiology

Published: March 12, 2025

Anti-band 3 and anti-spectrin antibodies are increased in Plasmodium vivax infection and are associated with anemia.

Anti-band 3 and anti-spectrin antibodies are increased in Plasmodium vivax infection and are associated with anemia.

Journal: Scientific reports

Published: January 10, 2018

Naturally Acquired Human Antibodies Against Reticulocyte-Binding Domains of Plasmodium vivax Proteins, PvRBP2c and PvRBP1a, Exhibit Binding-Inhibitory Activity.

Naturally Acquired Human Antibodies Against Reticulocyte-Binding Domains of Plasmodium vivax Proteins, PvRBP2c and PvRBP1a, Exhibit Binding-Inhibitory Activity.

Journal: The Journal of infectious diseases

Published: February 28, 2017

Multiple Plasmodium vivax proteins of Pv-fam-a family interact with human erythrocyte receptor Band 3 and have a role in red cell invasion.

Multiple Plasmodium vivax proteins of Pv-fam-a family interact with human erythrocyte receptor Band 3 and have a role in red cell invasion.

Journal: Biochemical and biophysical research communications

Published: July 02, 2016

Basigin Interacts with Plasmodium vivax Tryptophan-rich Antigen PvTRAg38 as a Second Erythrocyte Receptor to Promote Parasite Growth.

Basigin Interacts with Plasmodium vivax Tryptophan-rich Antigen PvTRAg38 as a Second Erythrocyte Receptor to Promote Parasite Growth.

Journal: The Journal of biological chemistry

Published: June 20, 2016

Receptor specific binding regions of Plasmodium vivax tryptophan rich antigens and parasite growth inhibition activity of PvTRAg35.2.

Receptor specific binding regions of Plasmodium vivax tryptophan rich antigens and parasite growth inhibition activity of PvTRAg35.2.

Journal: Microbes and infection

Published: January 21, 2016

Plasmodium vivax Tryptophan Rich Antigen PvTRAg36.6 Interacts with PvETRAMP and PvTRAg56.6 Interacts with PvMSP7 during Erythrocytic Stages of the Parasite.

Plasmodium vivax Tryptophan Rich Antigen PvTRAg36.6 Interacts with PvETRAMP and PvTRAg56.6 Interacts with PvMSP7 during Erythrocytic Stages of the Parasite.

Journal: PloS one

Published: November 06, 2015

Host-parasite interaction: multiple sites in the Plasmodium vivax tryptophan-rich antigen PvTRAg38 interact with the erythrocyte receptor band 3.

Host-parasite interaction: multiple sites in the Plasmodium vivax tryptophan-rich antigen PvTRAg38 interact with the erythrocyte receptor band 3.

Journal: FEBS letters

Published: August 13, 2015

Recognition of Human Erythrocyte Receptors by the Tryptophan-Rich Antigens of Monkey Malaria Parasite Plasmodium knowlesi.

Recognition of Human Erythrocyte Receptors by the Tryptophan-Rich Antigens of Monkey Malaria Parasite Plasmodium knowlesi.

Journal: PloS one

Published: May 20, 2015

Interaction of Plasmodium vivax Tryptophan-rich Antigen PvTRAg38 with Band 3 on Human Erythrocyte Surface Facilitates Parasite Growth.

Interaction of Plasmodium vivax Tryptophan-rich Antigen PvTRAg38 with Band 3 on Human Erythrocyte Surface Facilitates Parasite Growth.

Journal: The Journal of biological chemistry

Published: February 11, 2015

CD4+ T cell response correlates with naturally acquired antibodies against Plasmodium vivax tryptophan-rich antigens.

CD4+ T cell response correlates with naturally acquired antibodies against Plasmodium vivax tryptophan-rich antigens.

Journal: Infection and immunity

Published: December 18, 2014

Host-parasite interaction: selective Pv-fam-a family proteins of Plasmodium vivax bind to a restricted number of human erythrocyte receptors.

Host-parasite interaction: selective Pv-fam-a family proteins of Plasmodium vivax bind to a restricted number of human erythrocyte receptors.

Journal: The Journal of infectious diseases

Published: October 15, 2014

Showing 1-12 of 21

Last Updated: 09/26/2026