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Structural and antigenic characterization of Babesia Bovis HAP2 domains
by
Suarez, Carlos E.
, Rahman, S. M. Raihan
, Bastos, Reginaldo G.
, Ueti, Massaro W.
, Alzan, Heba F.
, Laughery, Jacob M.
in
631/114
/ 631/250
/ 631/326
/ 631/337
/ 631/601
/ 631/61
/ 692/699
/ Amino Acid Sequence
/ Animals
/ Antigenicity
/ Antigens, Protozoan - chemistry
/ Antigens, Protozoan - genetics
/ Antigens, Protozoan - immunology
/ Arabidopsis
/ Babesia Bovis
/ Babesia bovis - genetics
/ Babesia bovis - immunology
/ Babesiosis
/ Babesiosis - immunology
/ Babesiosis - parasitology
/ Babesiosis - prevention & control
/ Bovine babesiosis
/ Cattle
/ Cattle Diseases - immunology
/ Cattle Diseases - parasitology
/ Chlamydomonas reinhardtii
/ Disulfide bonds
/ Ectoparasites
/ HAP2
/ HAP2 domains
/ Hap2 protein
/ Humanities and Social Sciences
/ Immunization
/ Midgut
/ Models, Molecular
/ multidisciplinary
/ Parasites
/ Protein Domains
/ Proteins
/ Protozoan Proteins - chemistry
/ Protozoan Proteins - genetics
/ Protozoan Proteins - immunology
/ Science
/ Science (multidisciplinary)
/ Structural analysis
/ Transmission-blocking vaccine
/ Vaccines
2025
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Structural and antigenic characterization of Babesia Bovis HAP2 domains
by
Suarez, Carlos E.
, Rahman, S. M. Raihan
, Bastos, Reginaldo G.
, Ueti, Massaro W.
, Alzan, Heba F.
, Laughery, Jacob M.
in
631/114
/ 631/250
/ 631/326
/ 631/337
/ 631/601
/ 631/61
/ 692/699
/ Amino Acid Sequence
/ Animals
/ Antigenicity
/ Antigens, Protozoan - chemistry
/ Antigens, Protozoan - genetics
/ Antigens, Protozoan - immunology
/ Arabidopsis
/ Babesia Bovis
/ Babesia bovis - genetics
/ Babesia bovis - immunology
/ Babesiosis
/ Babesiosis - immunology
/ Babesiosis - parasitology
/ Babesiosis - prevention & control
/ Bovine babesiosis
/ Cattle
/ Cattle Diseases - immunology
/ Cattle Diseases - parasitology
/ Chlamydomonas reinhardtii
/ Disulfide bonds
/ Ectoparasites
/ HAP2
/ HAP2 domains
/ Hap2 protein
/ Humanities and Social Sciences
/ Immunization
/ Midgut
/ Models, Molecular
/ multidisciplinary
/ Parasites
/ Protein Domains
/ Proteins
/ Protozoan Proteins - chemistry
/ Protozoan Proteins - genetics
/ Protozoan Proteins - immunology
/ Science
/ Science (multidisciplinary)
/ Structural analysis
/ Transmission-blocking vaccine
/ Vaccines
2025
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Structural and antigenic characterization of Babesia Bovis HAP2 domains
by
Suarez, Carlos E.
, Rahman, S. M. Raihan
, Bastos, Reginaldo G.
, Ueti, Massaro W.
, Alzan, Heba F.
, Laughery, Jacob M.
in
631/114
/ 631/250
/ 631/326
/ 631/337
/ 631/601
/ 631/61
/ 692/699
/ Amino Acid Sequence
/ Animals
/ Antigenicity
/ Antigens, Protozoan - chemistry
/ Antigens, Protozoan - genetics
/ Antigens, Protozoan - immunology
/ Arabidopsis
/ Babesia Bovis
/ Babesia bovis - genetics
/ Babesia bovis - immunology
/ Babesiosis
/ Babesiosis - immunology
/ Babesiosis - parasitology
/ Babesiosis - prevention & control
/ Bovine babesiosis
/ Cattle
/ Cattle Diseases - immunology
/ Cattle Diseases - parasitology
/ Chlamydomonas reinhardtii
/ Disulfide bonds
/ Ectoparasites
/ HAP2
/ HAP2 domains
/ Hap2 protein
/ Humanities and Social Sciences
/ Immunization
/ Midgut
/ Models, Molecular
/ multidisciplinary
/ Parasites
/ Protein Domains
/ Proteins
/ Protozoan Proteins - chemistry
/ Protozoan Proteins - genetics
/ Protozoan Proteins - immunology
/ Science
/ Science (multidisciplinary)
/ Structural analysis
/ Transmission-blocking vaccine
/ Vaccines
2025
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Structural and antigenic characterization of Babesia Bovis HAP2 domains
Journal Article
Structural and antigenic characterization of Babesia Bovis HAP2 domains
2025
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Overview
The tick-borne apicomplexan parasite
Babesia bovis
causes bovine babesiosis which leads to enormous food and economic losses around the world. The existing resources to manage this disease are limited and have pitfalls, therefore, introduction of new strategies is urgently needed.
B. bovis
reproduces sexually in the midgut of its tick vector. HAP2, a well conserved ancient protein, plays a crucial role in the gamete fusion of this parasite and is a strong candidate for developing transmission-blocking vaccines. We previously demonstrated that immunization of cattle with full size
B. bovis
HAP2 blocks transmission of the parasite by
Rhipicephalus microplus
. Understanding the conserved structural features and antigenicity of HAP2 protein and its domains will facilitate developing effective methods to control pathogen transmission. In this study, we analyzed and compared AlphaFold2-predicted 3D structure of
B. bovis
HAP2 with the well-characterized crystal structures of HAP2 of
Chlamydomonas reinhardtii
and
Arabidopsis thaliana
. The comparisons and structural analysis resulted in the definition of three domains’ sequences, fusion loops, and disulfide bonds in the
B. bovis
HAP2. In addition, recombinant versions of each three predicted HAP2 domains were recognized by antibodies from HAP2 immunized and transmission-protected cattle, confirming their antigenicity. Remarkably, domain II was highly recognized compared to the other two domains. This study introduces new directions in designing novel functional assays and improved vaccine design through targeting the HAP2 protein.
Publisher
Nature Publishing Group UK,Nature Publishing Group,Nature Portfolio
Subject
/ 631/250
/ 631/326
/ 631/337
/ 631/601
/ 631/61
/ 692/699
/ Animals
/ Antigens, Protozoan - chemistry
/ Antigens, Protozoan - genetics
/ Antigens, Protozoan - immunology
/ Babesiosis - prevention & control
/ Cattle
/ Cattle Diseases - immunology
/ Cattle Diseases - parasitology
/ HAP2
/ Humanities and Social Sciences
/ Midgut
/ Proteins
/ Protozoan Proteins - chemistry
/ Protozoan Proteins - genetics
/ Protozoan Proteins - immunology
/ Science
/ Transmission-blocking vaccine
/ Vaccines
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