PMID- 35463644
OWN - NLM
STAT- MEDLINE
DCOM- 20220426
LR  - 20220716
IS  - 2235-2988 (Electronic)
IS  - 2235-2988 (Linking)
VI  - 12
DP  - 2022
TI  - Thrombospondin Related Anonymous Protein Superfamily in Vector-Borne 
      Apicomplexans: The Parasite's Toolkit for Cell Invasion.
PG  - 831592
LID - 10.3389/fcimb.2022.831592 [doi]
LID - 831592
AB  - Apicomplexan parasites transmitted by vectors, including Babesia spp. and 
      Plasmodium spp., cause severe disease in both humans and animals. These parasites 
      have a complex life cycle during which they migrate, invade, and replicate in 
      contrasting hosts such as the mammal and the invertebrate vector. The interaction 
      of parasites with the host cell is mediated by adhesive proteins which play a key 
      role in the different cellular processes regarding successful progression of the 
      life cycle. Thrombospondin related anonymous protein (TRAP) is a superfamily of 
      adhesins that are involved in motility, invasion and egress of the parasite. 
      These proteins are stored and released from apical organelles and have either one 
      or two types of adhesive domains, namely thrombospondin type 1 repeat and von 
      Willebrand factor type A, that upon secretion are located in the extracellular 
      portion of the molecule. Proteins from the TRAP superfamily have been intensively 
      studied in Plasmodium species and to a lesser extent in Babesia spp., where they 
      have proven to be functionally relevant throughout the entire parasite's journey 
      both in the arthropod vector and in the mammalian host. In recent years new 
      findings provided answers to the role of TRAP proteins and in some cases the 
      function of these adhesins during the parasite's life cycle was redefined. In 
      this review we will discuss the current knowledge of the diverse roles of the 
      TRAP superfamily in vector-borne parasites from Class Aconoidasida. We will focus 
      on the varied approaches that allowed the understanding of protein function and 
      the relevance of TRAP- superfamily throughout the entire parasite's cell cycle.
CI  - Copyright (c) 2022 Paoletta and Wilkowsky.
FAU - Paoletta, Martina Soledad
AU  - Paoletta MS
AD  - Instituto de Agrobiotecnologia y Biologia Molecular (IABIMO), Instituto Nacional 
      de Tecnologia Agropecuaria (INTA) - Consejo Nacional de Investigaciones 
      Cientificas y Tecnicas (CONICET), Hurlingham, Argentina.
FAU - Wilkowsky, Silvina Elizabeth
AU  - Wilkowsky SE
AD  - Instituto de Agrobiotecnologia y Biologia Molecular (IABIMO), Instituto Nacional 
      de Tecnologia Agropecuaria (INTA) - Consejo Nacional de Investigaciones 
      Cientificas y Tecnicas (CONICET), Hurlingham, Argentina.
LA  - eng
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PT  - Review
DEP - 20220406
PL  - Switzerland
TA  - Front Cell Infect Microbiol
JT  - Frontiers in cellular and infection microbiology
JID - 101585359
RN  - 0 (Protozoan Proteins)
RN  - 0 (Thrombospondins)
SB  - IM
MH  - Animals
MH  - *Babesia/genetics
MH  - Mammals/metabolism
MH  - *Parasites/metabolism
MH  - *Plasmodium/metabolism
MH  - Protozoan Proteins/genetics/metabolism
MH  - Thrombospondins
PMC - PMC9019593
OTO - NOTNLM
OT  - Babesia
OT  - Plasmodium
OT  - TRAP family
OT  - TRP family
OT  - adhesive domains
OT  - thrombospondin type 1 repeat
OT  - thrombospondin-related anonymous protein
OT  - von Willebrand factor type A
COIS- The authors declare that the research was conducted in the absence of any 
      commercial or financial relationships that could be construed as a potential 
      conflict of interest.
EDAT- 2022/04/26 06:00
MHDA- 2022/04/27 06:00
PMCR- 2022/01/01
CRDT- 2022/04/25 05:22
PHST- 2021/12/08 00:00 [received]
PHST- 2022/03/07 00:00 [accepted]
PHST- 2022/04/25 05:22 [entrez]
PHST- 2022/04/26 06:00 [pubmed]
PHST- 2022/04/27 06:00 [medline]
PHST- 2022/01/01 00:00 [pmc-release]
AID - 10.3389/fcimb.2022.831592 [doi]
PST - epublish
SO  - Front Cell Infect Microbiol. 2022 Apr 6;12:831592. doi: 
      10.3389/fcimb.2022.831592. eCollection 2022.