Toxoplasma gondii SAG1 targeting host cell S100A6 for parasite invasion and host immunity

Zhou, Lijuan; Peng, Jiao; Chen, Min; Yao, Lijie; Zou, Wei; He, Cynthia Y.; Peng, Hong‐Juan

doi:10.1016/j.isci.2021.103514

Cited by 11 publications

(6 citation statements)

References 56 publications

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“…In 2022, Hollstein et al demonstrated the application of TurboID in the filamentous fungus Sordaria macrospora (Sm) using the striatin-interacting phosphatase and kinase complex (SmSTRIPAK). They fused codon-optimized TurboID biotin ligase with striatin-interacting phosphatase and kinase (STRIPAK) complex 1 (SCI1) and identified known SmSTRIPAK components (PRO11, SmMOB3, PRO22, and SmPP2Ac1) through affinity purification and mass spectrometry, indicating the successful application of TurboID in filamentous fungi [ 139 ].…”

Section: Applications Of Biotin Ligase-based Proximity Marker Technologymentioning

confidence: 99%

The development of proximity labeling technology and its applications in mammals, plants, and microorganisms

Guo,

et al. 2023

Cell Commun Signal

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Protein‒protein, protein‒RNA, and protein‒DNA interaction networks form the basis of cellular regulation and signal transduction, making it crucial to explore these interaction networks to understand complex biological processes. Traditional methods such as affinity purification and yeast two-hybrid assays have been shown to have limitations, as they can only isolate high-affinity molecular interactions under nonphysiological conditions or in vitro. Moreover, these methods have shortcomings for organelle isolation and protein subcellular localization. To address these issues, proximity labeling techniques have been developed. This technology not only overcomes the limitations of traditional methods but also offers unique advantages in studying protein spatial characteristics and molecular interactions within living cells. Currently, this technique not only is indispensable in research on mammalian nucleoprotein interactions but also provides a reliable approach for studying nonmammalian cells, such as plants, parasites and viruses. Given these advantages, this article provides a detailed introduction to the principles of proximity labeling techniques and the development of labeling enzymes. The focus is on summarizing the recent applications of TurboID and miniTurbo in mammals, plants, and microorganisms.

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Section: Applications Of Biotin Ligase-based Proximity Marker Technologymentioning

confidence: 99%

The development of proximity labeling technology and its applications in mammals, plants, and microorganisms

Guo,

et al. 2023

Cell Commun Signal

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“…Given that we were unable to identify KASH domain proteins with standard bioinformatic approaches in T. gondii , it seems likely that the SUN-binding counterpart is an atypical KASH-like protein, similar to what has been observed in other organisms. In an attempt to identify potential interaction partners of TgSLP1, we used proximity labelling (TurboID; Branon et al, 2018 ; Zhou et al, 2021 ), but due to inconsistent results, no KASH-like protein could be identified using this method (data not shown). Based on an educated guess, we studied two hypothetical proteins ( and ) with negative phenotypic scores ( Sidik et al, 2016 ) for their subcellular localisation.…”

Section: Discussionmentioning

confidence: 99%

The SUN-like protein TgSLP1 is essential for nuclear division in the apicomplexan parasite Toxoplasma gondii

Wagner,

Song,

Jiménez-Ruiz

et al. 2023

Journal of Cell Science

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Connections between the nucleus and the cytoskeleton are important for positioning and division of the nucleus. In most eukaryotes, the linker of nucleoskeleton and cytoskeleton (LINC) complex spans the outer and inner nuclear membranes and connects the nucleus to the cytoskeleton. In opisthokonts, it is composed of Klarsicht, ANC-1 and Syne homology (KASH) domain proteins and Sad1 and UNC-84 (SUN) domain proteins. Given that the nucleus is positioned at the posterior pole of Toxoplasma gondii, we speculated that apicomplexan parasites must have a similar mechanism that integrates the nucleus and the cytoskeleton. Here, we identified three UNC family proteins in the genome of the apicomplexan parasite T. gondii. Whereas the UNC-50 protein TgUNC1 localised to the Golgi and appeared to be not essential for the parasite, the SUN domain protein TgSLP2 showed a diffuse pattern throughout the parasite. The second SUN domain protein, TgSLP1, was expressed in a cell cycle-dependent manner and was localised close to the mitotic spindle and, more detailed, at the kinetochore. We demonstrate that conditional knockout of TgSLP1 leads to failure of nuclear division and loss of centrocone integrity.

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“…Osteosarcoma [29] Pancreatic cancer [30] Alzheimer's disease [31] Potential therapeutic target for acute myocardial infarction [32] Neurodegenerative diseases [33] Veterinary studies: Porcine reproductive and respiratory syndrome virus [34] Atopic dogs [35] Toxoplasma gondii infection [36] S100A7 (Psoriasin1) Psoriasis and inflammatory skin diseases [37] Squamous cell carcinomas and large cell lung carcinomas [38] Alzheimer disease [39] Wound healing process [40] Role in breast cancer [41] Veterinary studies: Mastitis in goat [42] Use of fecal calprotectin [43] Biological function and use as biomarker [44] Diagnosis of sepsis [45] S100A10 (Calpactin-1 Plasminogen receptor S100A10)…”

Section: S100a6 [Calcyclin (Cacy)]mentioning

confidence: 99%

S-100 Proteins: Basics and Applications as Biomarkers in Animals with Special Focus on Calgranulins (S100A8, A9, and A12)

Cerón

Ortín-Bustillo

López-Martínez

et al. 2023

Biology

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S100 proteins are a group of calcium-binding proteins which received this name because of their solubility in a 100% saturated solution of ammonium sulphate. They have a similar molecular mass of 10–12 KDa and share 25–65% similarity in their amino acid sequence. They are expressed in many tissues, and to date 25 different types of S100 proteins have been identified. This review aims to provide updated information about S100 proteins and their use as biomarkers in veterinary science, with special emphasis on the family of calgranulins that includes S100A8 (calgranulin A; myeloid-related protein 8, MRP8), S100A9 (calgranulin B; MRP14), and S100A12 (calgranulin C). The proteins SA100A8 and S100A9 can be linked, forming a heterodimer which is known as calprotectin. Calgranulins are related to the activation of inflammation and the immune system and increase in gastrointestinal diseases, inflammation and sepsis, immunomediated diseases, and obesity and endocrine disorders in different animal species. This review reflects the current knowledge about calgranulins in veterinary science, which should increase in the future to clarify their role in different diseases and potential as biomarkers and therapeutic targets, as well as the practical use of their measurement in non-invasive samples such as saliva or feces.

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Toxoplasma gondii SAG1 targeting host cell S100A6 for parasite invasion and host immunity

Cited by 11 publications

References 56 publications

The development of proximity labeling technology and its applications in mammals, plants, and microorganisms

The development of proximity labeling technology and its applications in mammals, plants, and microorganisms

The SUN-like protein TgSLP1 is essential for nuclear division in the apicomplexan parasite Toxoplasma gondii

S-100 Proteins: Basics and Applications as Biomarkers in Animals with Special Focus on Calgranulins (S100A8, A9, and A12)

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