Characterization of a candidate gene for GP72, an insect stage-specific antigen ofTrypanosoma cruzi

Cooper, Robin; Inverso, J A; Espinosa, Martha; Nogueira, N; Cross, George A.M.

doi:10.1016/0166-6851(91)90129-t

Cited by 34 publications

(21 citation statements)

References 39 publications

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“…Thus, for example, the E13 element which was found to represent approximately 7% of the total nuclear DNA from the parasite [7] is distributed over most of the chromosomes. Fragments homologous to the E13 element have been described to be present in the 24S rDNA pseudogene [8] and in the region located upstream from the splicing acceptor site of the stage-specific antigen GP72 gene [9]. Also, the short interspersed nucleotide element (SINE) has been described to be present in the intergenic region of certain P2û genes [10] and in the 3©-end of some H2A gene units [11].…”

Section: Introductionmentioning

confidence: 99%

Genomic clustering of theTrypanosoma cruzi nonlong terminal L1Tc retrotransposon with defined interspersed repeated DNA elements

et al. 2000

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We have analyzed the genomic distribution and organization of the long interspersed nucleotide element (LINE) L1Tc, a nonlong terminal repeat (LTR) retrotransposon of Trypanosoma cruzi. The results indicate that the L1Tc element is dispersed along the parasite genome and that in some regions it is organized in tandem repeats. The data allowed us to define the existence of short direct-repeated sequences flanking the genomic L1Tc elements. Relevant is the finding that the LINE L1Tc is located in genomic regions rich in short interspersed nucleotide elements (SINE)-like sequences. In particular, the L1Tc element is found associated to E13-related sequences, redefined in this work and renamed RS13Tc, and to a newly described RS1Tc sequence. The RS1Tc sequence is present, per haploid genome, in about 3,200 copies. Northern blot analysis showed that the RS1Tc is being transcribed into RNAs of different sizes. The analysis of the chromosomal distribution of these elements in various strains of T. cruzi suggested that this type of clustering might be a common feature of the genome of these parasites.

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Section: Introductionmentioning

confidence: 99%

Genomic clustering of theTrypanosoma cruzi nonlong terminal L1Tc retrotransposon with defined interspersed repeated DNA elements

et al. 2000

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“…The first such molecule characterized was GP72, a stage-specific, glycosylated membrane protein in T. cruzi (Cooper et al, 1991). GP72 was readily detected along the flagellum adjacent to the adhesion region using indirect immunofluorescence on live, nonpermeabilized parasites .…”

Section: Introductionmentioning

confidence: 99%

An intracellular membrane junction consisting of flagellum adhesion glycoproteins links flagellum biogenesis to cell morphogenesis in Trypanosoma brucei

Sun

Wang

Yuan

et al. 2013

Journal of Cell Science

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SummaryAfrican trypanosomes have a single, membrane-bounded flagellum that is attached to the cell cortex by membrane adhesion proteins and an intracellular flagellum attachment zone (FAZ) complex. The coordinated assembly of flagellum and FAZ, during the cell cycle and the life cycle development, plays a pivotal role in organelle positioning, cell division and cell morphogenesis. To understand how the flagellum and FAZ assembly are coordinated, we examined the domain organization of the flagellum adhesion protein 1 (FLA1), a glycosylated, transmembrane protein essential for flagellum attachment and cell division. By immunoprecipitation of a FLA1-truncation mutant that mislocalized to the flagellum, a novel FLA1-binding protein (FLA1BP) was identified in procyclic Trypanosoma brucei. The interaction between FLA1 on the cell membrane and FLA1BP on the flagellum membrane acts like a molecular zipper, joining flagellum membrane to cell membrane and linking flagellum biogenesis to FAZ elongation. By coordinating flagellum and FAZ assembly during the cell cycle, morphology information is transmitted from the flagellum to the cell body.

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“…Another family of proteins involved in flagellum attachment comprises transmembrane proteins. The first member was discovered in Trypanosoma cruzi as a glycoprotein named GP72, which contains a C-terminal short cytoplasmic sequence, a transmembrane domain and a large extracellular portion that is heavily glycosylated (Cooper et al, 1991). It is conserved in T. brucei as a 546 amino acid transmembrane glycoprotein called FLA1 composed of a short intra-cellular C-terminal end (16 aa) and a long N-and O-glycosylated N-terminal extracellular tail (475 aa).…”

Section: Introductionmentioning

confidence: 99%

Flagellar adhesion inTrypanosoma bruceirelies on interactions between different skeletal structures present in the flagellum and in the cell body

Rotureau

Blisnick

Subota

et al. 2013

Journal of Cell Science

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The Trypanosoma brucei flagellum is an essential organelle anchored along the surface of the cell body through a specialized structure called the flagellum attachment zone (FAZ). Adhesion relies on the interaction of the extracellular portion of two transmembrane proteins, FLA1 and FLA1BP. Here, we identify FLAM3 as a novel large protein associated with the flagellum skeleton whose ablation inhibits flagellum attachment. FLAM3 does not contain transmembrane domains and its flagellar localization matches closely, but not exactly, that of the paraflagellar rod, an extraaxonemal structure present in the flagellum. Knockdown of FLA1 or FLAM3 triggers similar defects in motility and morphogenesis, characterized by the assembly of a drastically reduced FAZ filament. FLAM3 remains associated with the flagellum skeleton even in the absence of adhesion or a normal paraflagellar rod. However, the protein is dispersed in the cytoplasm when flagellum formation is inhibited. By contrast, FLA1 remains tightly associated with the FAZ filament even in the absence of a flagellum. In these conditions, the extracellular domain of FLA1 points to the cell surface. FLAM3 is essential for proper distribution of FLA1BP, which is restricted to the most proximal portion of the flagellum upon knockdown of FLAM3. We propose that FLAM3 is a key component of the FAZ connectors that link the axoneme to the adhesion zone, hence it acts in an equivalent manner to the FAZ filament complex, but on the side of the flagellum.

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Characterization of a candidate gene for GP72, an insect stage-specific antigen ofTrypanosoma cruzi

Cited by 34 publications

References 39 publications

Genomic clustering of theTrypanosoma cruzi nonlong terminal L1Tc retrotransposon with defined interspersed repeated DNA elements

Genomic clustering of theTrypanosoma cruzi nonlong terminal L1Tc retrotransposon with defined interspersed repeated DNA elements

An intracellular membrane junction consisting of flagellum adhesion glycoproteins links flagellum biogenesis to cell morphogenesis in Trypanosoma brucei

Flagellar adhesion inTrypanosoma bruceirelies on interactions between different skeletal structures present in the flagellum and in the cell body

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