<i>Babesia microti</i> Immunoreactive Rhoptry-Associated Protein-1 Paralogs Are Ancestral Members of the Piroplasmid-Confined RAP-1 Family
<i>Babesia</i>, <i>Cytauxzoon</i> and <i>Theileria</i> are tick-borne apicomplexan parasites of the order Piroplasmida, responsible for diseases in humans and animals. Members of the piroplasmid rhoptry-associated protein-1 (pRAP-1) family have a signature cystein...
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oai:doaj.org-article:ed63503e46424a4eb897d5dc6b37d5372021-11-25T18:37:49Z<i>Babesia microti</i> Immunoreactive Rhoptry-Associated Protein-1 Paralogs Are Ancestral Members of the Piroplasmid-Confined RAP-1 Family10.3390/pathogens101113842076-0817https://doaj.org/article/ed63503e46424a4eb897d5dc6b37d5372021-10-01T00:00:00Zhttps://www.mdpi.com/2076-0817/10/11/1384https://doaj.org/toc/2076-0817<i>Babesia</i>, <i>Cytauxzoon</i> and <i>Theileria</i> are tick-borne apicomplexan parasites of the order Piroplasmida, responsible for diseases in humans and animals. Members of the piroplasmid rhoptry-associated protein-1 (pRAP-1) family have a signature cysteine-rich domain and are important for parasite development. We propose that the closely linked <i>B. microti</i> genes annotated as BMR1_03g00947 and BMR1_03g00960 encode two paralogue pRAP-1-like proteins named BmIPA48 and Bm960. The two genes are tandemly arranged head to tail, highly expressed in blood stage parasites, syntenic to <i>rap-1</i> genes of other piroplasmids, and share large portions of an almost identical ~225 bp sequence located in their 5′ putative regulatory regions. BmIPA48 and Bm960 proteins contain a N-terminal signal peptide, share very low sequence identity (<13%) with pRAP-1 from other species, and harbor one or more transmembrane domains. Diversification of the piroplasmid-confined <i>prap-1</i> family is characterized by amplification of genes, protein domains, and a high sequence polymorphism. This suggests a functional involvement of pRAP-1 at the parasite-host interface, possibly in parasite adhesion, attachment, and/or evasion of the host immune defenses. Both BmIPA48 and Bm960 are recognized by antibodies in sera from humans infected with <i>B. microti</i> and might be promising candidates for developing novel serodiagnosis and vaccines.Reginaldo G. BastosJose ThekkiniathChoukri Ben MamounLee FullerRobert E. MolestinaMonica Florin-ChristensenLeonhard SchnittgerHeba F. AlzanCarlos E. SuarezMDPI AGarticle<i>Babesia microti</i>BmIPA48BMR1_03g00960piroplasmid rhoptry-associated protein-1 (pRAP-1)human babesiosisMedicineRENPathogens, Vol 10, Iss 1384, p 1384 (2021) |
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<i>Babesia microti</i> BmIPA48 BMR1_03g00960 piroplasmid rhoptry-associated protein-1 (pRAP-1) human babesiosis Medicine R |
spellingShingle |
<i>Babesia microti</i> BmIPA48 BMR1_03g00960 piroplasmid rhoptry-associated protein-1 (pRAP-1) human babesiosis Medicine R Reginaldo G. Bastos Jose Thekkiniath Choukri Ben Mamoun Lee Fuller Robert E. Molestina Monica Florin-Christensen Leonhard Schnittger Heba F. Alzan Carlos E. Suarez <i>Babesia microti</i> Immunoreactive Rhoptry-Associated Protein-1 Paralogs Are Ancestral Members of the Piroplasmid-Confined RAP-1 Family |
description |
<i>Babesia</i>, <i>Cytauxzoon</i> and <i>Theileria</i> are tick-borne apicomplexan parasites of the order Piroplasmida, responsible for diseases in humans and animals. Members of the piroplasmid rhoptry-associated protein-1 (pRAP-1) family have a signature cysteine-rich domain and are important for parasite development. We propose that the closely linked <i>B. microti</i> genes annotated as BMR1_03g00947 and BMR1_03g00960 encode two paralogue pRAP-1-like proteins named BmIPA48 and Bm960. The two genes are tandemly arranged head to tail, highly expressed in blood stage parasites, syntenic to <i>rap-1</i> genes of other piroplasmids, and share large portions of an almost identical ~225 bp sequence located in their 5′ putative regulatory regions. BmIPA48 and Bm960 proteins contain a N-terminal signal peptide, share very low sequence identity (<13%) with pRAP-1 from other species, and harbor one or more transmembrane domains. Diversification of the piroplasmid-confined <i>prap-1</i> family is characterized by amplification of genes, protein domains, and a high sequence polymorphism. This suggests a functional involvement of pRAP-1 at the parasite-host interface, possibly in parasite adhesion, attachment, and/or evasion of the host immune defenses. Both BmIPA48 and Bm960 are recognized by antibodies in sera from humans infected with <i>B. microti</i> and might be promising candidates for developing novel serodiagnosis and vaccines. |
format |
article |
author |
Reginaldo G. Bastos Jose Thekkiniath Choukri Ben Mamoun Lee Fuller Robert E. Molestina Monica Florin-Christensen Leonhard Schnittger Heba F. Alzan Carlos E. Suarez |
author_facet |
Reginaldo G. Bastos Jose Thekkiniath Choukri Ben Mamoun Lee Fuller Robert E. Molestina Monica Florin-Christensen Leonhard Schnittger Heba F. Alzan Carlos E. Suarez |
author_sort |
Reginaldo G. Bastos |
title |
<i>Babesia microti</i> Immunoreactive Rhoptry-Associated Protein-1 Paralogs Are Ancestral Members of the Piroplasmid-Confined RAP-1 Family |
title_short |
<i>Babesia microti</i> Immunoreactive Rhoptry-Associated Protein-1 Paralogs Are Ancestral Members of the Piroplasmid-Confined RAP-1 Family |
title_full |
<i>Babesia microti</i> Immunoreactive Rhoptry-Associated Protein-1 Paralogs Are Ancestral Members of the Piroplasmid-Confined RAP-1 Family |
title_fullStr |
<i>Babesia microti</i> Immunoreactive Rhoptry-Associated Protein-1 Paralogs Are Ancestral Members of the Piroplasmid-Confined RAP-1 Family |
title_full_unstemmed |
<i>Babesia microti</i> Immunoreactive Rhoptry-Associated Protein-1 Paralogs Are Ancestral Members of the Piroplasmid-Confined RAP-1 Family |
title_sort |
<i>babesia microti</i> immunoreactive rhoptry-associated protein-1 paralogs are ancestral members of the piroplasmid-confined rap-1 family |
publisher |
MDPI AG |
publishDate |
2021 |
url |
https://doaj.org/article/ed63503e46424a4eb897d5dc6b37d537 |
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