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Journal articles on the topic 'Gamma‐interferon‐inducible lysosomal Thiol Reductase'

Author: Grafiati

Published: 4 June 2021

Last updated: 3 February 2022

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1

Nguyen, Jennifer, Richard Bernert, Kevin In, Paul Kang, Noemi Sebastiao, Chengcheng Hu, and K. Taraszka Hastings. "Gamma-interferon-inducible lysosomal thiol reductase is upregulated in human melanoma." Melanoma Research 26, no. 2 (April 2016): 125–37. http://dx.doi.org/10.1097/cmr.0000000000000230.

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2

Zhou, Lidan, Weili Yan, Lin Yang, Hui Chen, Qianqian Cao, and Wenhua Ren. "Isolation of gamma-interferon-inducible lysosomal thiol reductase (GILT) from the Yangtze finless porpoise." Developmental & Comparative Immunology 41, no. 4 (December 2013): 652–56. http://dx.doi.org/10.1016/j.dci.2013.06.012.

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3

Arunachalam, B., U. T. Phan, H. J. Geuze, and P. Cresswell. "Enzymatic reduction of disulfide bonds in lysosomes: Characterization of a Gamma-interferon-inducible lysosomal thiol reductase (GILT)." Proceedings of the National Academy of Sciences 97, no. 2 (January 18, 2000): 745–50. http://dx.doi.org/10.1073/pnas.97.2.745.

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4

Hastings, Karen Taraszka, and Peter Cresswell. "Disulfide Reduction in the Endocytic Pathway: Immunological Functions of Gamma-Interferon-Inducible Lysosomal Thiol Reductase." Antioxidants & Redox Signaling 15, no. 3 (August 2011): 657–68. http://dx.doi.org/10.1089/ars.2010.3684.

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5

In, K., H. Menon, J. Nguyen, N. Sebastiao, P. Kang, C. Hu, R. Bernert, D. J. DiCaudo, and K. T. Hastings. "290 Gamma-interferon-inducible lysosomal thiol reductase is upregulated in human melanoma and halo nevi." Journal of Investigative Dermatology 136, no. 5 (May 2016): S51. http://dx.doi.org/10.1016/j.jid.2016.02.320.

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6

Gao, Lili, Ao Li, Yanhua Lv, Mujie Huang, Xi Liu, Hongkuan Deng, Dongwu Liu, Bosheng Zhao, Baohua Liu, and Qiuxiang Pang. "Planarian gamma-interferon-inducible lysosomal thiol reductase (GILT) is required for gram-negative bacterial clearance." Developmental & Comparative Immunology 116 (March 2021): 103914. http://dx.doi.org/10.1016/j.dci.2020.103914.

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7

Cao, Fang, Haitao Wu, Tongtong Lv, Yunqing Yang, Yue Li, Shuaimei Liu, Lingling Hu, et al. "Molecular and biological characterization of gamma-interferon-inducible lysosomal thiol reductase in silver carp (Hypophthalmichthys molitrix)." Fish & Shellfish Immunology 79 (August 2018): 73–78. http://dx.doi.org/10.1016/j.fsi.2018.04.064.

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8

Ren, Chunhua, Ting Chen, Xiao Jiang, Xing Luo, Yanhong Wang, and Chaoqun Hu. "The first echinoderm gamma-interferon-inducible lysosomal thiol reductase (GILT) identified from sea cucumber (Stichopus monotuberculatus)." Fish & Shellfish Immunology 42, no. 1 (January 2015): 41–49. http://dx.doi.org/10.1016/j.fsi.2014.10.024.

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9

Kongton, Kittima, Kimberly McCall, and Amornrat Phongdara. "Identification of gamma-interferon-inducible lysosomal thiol reductase (GILT) homologues in the fruit fly Drosophila melanogaster." Developmental & Comparative Immunology 44, no. 2 (June 2014): 389–96. http://dx.doi.org/10.1016/j.dci.2014.01.007.

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10

Srinivasan, Priya, and Maja Maric. "Signal transducer and activator of transcription 1 negatively regulates constitutive gamma interferon-inducible lysosomal thiol reductase expression." Immunology 132, no. 2 (October 13, 2010): 209–16. http://dx.doi.org/10.1111/j.1365-2567.2010.03355.x.

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11

Ma, Lei, Fang Cao, Runze Tang, Jiaxin Zhang, and Shuangquan Zhang. "Identification and characterization of a gamma-interferon-inducible lysosomal thiol reductase homolog from guinea pig ( Cavia porcellus ) that exhibits thiol reductase activity in vitro." Research in Veterinary Science 111 (April 2017): 81–84. http://dx.doi.org/10.1016/j.rvsc.2016.12.006.

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12

Satoh, Jun-ichi, Yoshihiro Kino, Motoaki Yanaizu, Tsuyoshi Ishida, and Yuko Saito. "Microglia express gamma-interferon-inducible lysosomal thiol reductase in the brains of Alzheimer's disease and Nasu-Hakola disease." Intractable & Rare Diseases Research 7, no. 4 (November 30, 2018): 251–57. http://dx.doi.org/10.5582/irdr.2018.01119.

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13

Liu, Min, Li Liu, Muhammad Nadeem Abbas, Saima Kausar, Jun-Wei Zhang, Zhi-Ze Ye, Xing-Yi Qian, Xiao-Ming Zhao, Sheng-Hui Chu, and Li-Shang Dai. "Involvement of gamma interferon inducible lysosomal thiol reductase in the innate immune responses of red swamp crayfish, Procambarus clarkii." Developmental & Comparative Immunology 99 (October 2019): 103405. http://dx.doi.org/10.1016/j.dci.2019.103405.

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14

Xiang, Yu-Juan, Ming-Ming Guo, Cheng-Jun Zhou, Lu Liu, Bo Han, Ling-Yu Kong, Zhong-Cheng Gao, et al. "Absence of Gamma-Interferon-Inducible Lysosomal Thiol Reductase (GILT) Is Associated with Poor Disease-Free Survival in Breast Cancer Patients." PLoS ONE 9, no. 10 (October 21, 2014): e109449. http://dx.doi.org/10.1371/journal.pone.0109449.

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15

Yang, Qian, Jiaxin Zhang, Lingling Hu, Jia Lu, Ming Sang, and Shuangquan Zhang. "Molecular structure and functional characterization of the gamma-interferon-inducible lysosomal thiol reductase (GILT) gene in largemouth bass (Microptenus salmoides)." Fish & Shellfish Immunology 47, no. 2 (December 2015): 689–96. http://dx.doi.org/10.1016/j.fsi.2015.10.018.

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16

Norton, Duncan L., and Azizul Haque. "Insights into the Role of GILT in HLA Class II Antigen Processing and Presentation by Melanoma." Journal of Oncology 2009 (2009): 1–8. http://dx.doi.org/10.1155/2009/142959.

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Metastatic melanoma is one of the deadliest of skin cancers and is increasing in incidence. Since current treatment regimens are ineffective at controlling and/or curing the disease, novel approaches, such as immunotherapy, for treating this malignant disease are being explored. In this review, we discuss potential melanoma antigens (Ags) and their role in utilizing the HLA class II pathway to elicit tumor Ag-specificCD4+T cell responses in order to effectively induce long-lastingCD8+antitumor memory. We also discuss the role of endolysosomal cathepsins and Gamma-Interferon-inducible Lysosomal Thiol reductase (GILT) in Ag processing and presentation, and at enhancingCD4+T cell recognition of melanoma cells. This review also summarizes our current knowledge on GILT and highlights a novel mechanism of GILT-mediated immune responses against melanoma cells. At the end, we propose a strategy employing GILT in the development of a potential whole cell vaccine for combating metastatic melanoma.

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17

Liu, Naiguo, Shicui Zhang, Zhenhui Liu, Saren Gaowa, and Yongjun Wang. "Characterization and expression of gamma-interferon-inducible lysosomal thiol reductase (GILT) gene in amphioxus Branchiostoma belcheri with implications for GILT in innate immune response." Molecular Immunology 44, no. 10 (April 2007): 2631–37. http://dx.doi.org/10.1016/j.molimm.2006.12.013.

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18

Liu, Meng, Hongyan Liu, Xiaocui Guan, Hongxin Ai, Haitao Wu, Ping Liu, Wei Gu, and Shuangquan Zhang. "Characterization and expression of gamma-interferon-inducible lysosomal thiol reductase (GILT) gene in rainbow trout (Oncorhynchus mykiss) with implications for GILT in innate immune response." Immunogenetics 65, no. 12 (September 5, 2013): 873–82. http://dx.doi.org/10.1007/s00251-013-0701-1.

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19

Dan, Wen-Bing, Shu-Le Wang, Jun-Qing Liang, and Shuang-Quan Zhang. "Molecular cloning and expression analysis of porcine γ-interferon-inducible lysosomal thiol reductase (GILT)." Veterinary Immunology and Immunopathology 126, no. 1-2 (November 2008): 163–67. http://dx.doi.org/10.1016/j.vetimm.2008.06.009.

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20

Balce, Dale R., Euan R. O. Allan, Neil McKenna, and Robin M. Yates. "γ-Interferon-inducible Lysosomal Thiol Reductase (GILT) Maintains Phagosomal Proteolysis in Alternatively Activated Macrophages." Journal of Biological Chemistry 289, no. 46 (September 24, 2014): 31891–904. http://dx.doi.org/10.1074/jbc.m114.584391.

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21

Ewanchuk, Benjamin W., Corey R. Arnold, Dale R. Balce, Priyatha Premnath, Tanis L. Orsetti, Amy L. Warren, Alexandra Olsen, Roman J. Krawetz, and Robin M. Yates. "A non-immunological role for γ-interferon–inducible lysosomal thiol reductase (GILT) in osteoclastic bone resorption." Science Advances 7, no. 17 (April 2021): eabd3684. http://dx.doi.org/10.1126/sciadv.abd3684.

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The extracellular bone resorbing lacuna of the osteoclast shares many characteristics with the degradative lysosome of antigen-presenting cells. γ-Interferon–inducible lysosomal thiol reductase (GILT) enhances antigen processing within lysosomes through direct reduction of antigen disulfides and maintenance of cysteine protease activity. In this study, we found the osteoclastogenic cytokine RANKL drove expression of GILT in osteoclast precursors in a STAT1-dependent manner, resulting in high levels of GILT in mature osteoclasts, which could be further augmented by γ-interferon. GILT colocalized with the collagen-degrading cysteine protease, cathepsin K, suggesting a role for GILT inside the osteoclastic resorption lacuna. GILT-deficient osteoclasts had reduced bone-resorbing capacity, resulting in impaired bone turnover and an osteopetrotic phenotype in GILT-deficient mice. We demonstrated that GILT could directly reduce the noncollagenous bone matrix protein SPARC, and additionally, enhance collagen degradation by cathepsin K. Together, this work describes a previously unidentified, non-immunological role for GILT in osteoclast-mediated bone resorption.

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22

Chen, Sansong, Qifu Wang, Xuefei Shao, Guangfu Di, Yi Dai, Xiaochun Jiang, and Limin Cheng. "Lentivirus mediated γ-interferon-inducible lysosomal thiol reductase (GILT) knockdown suppresses human glioma U373MG cell proliferation." Biochemical and Biophysical Research Communications 509, no. 1 (January 2019): 182–87. http://dx.doi.org/10.1016/j.bbrc.2018.12.099.

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23

Cui, Xian-wei, Chen-bo Ji, Xin-guo Cao, Zi-yi Fu, Shuang-quan Zhang, and Xi-rong Guo. "Molecular and biological characterization of interferon-γ-inducible-lysosomal thiol reductase gene in zebrafish (Danio rerio)." Fish & Shellfish Immunology 33, no. 5 (November 2012): 1133–38. http://dx.doi.org/10.1016/j.fsi.2012.08.021.

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24

Goldstein, Oliver G., Laela M. Hajiaghamohseni, Shereen Amria, Kumaran Sundaram, Sakamuri V. Reddy, and Azizul Haque. "Gamma-IFN-inducible-lysosomal thiol reductase modulates acidic proteases and HLA class II antigen processing in melanoma." Cancer Immunology, Immunotherapy 57, no. 10 (March 15, 2008): 1461–70. http://dx.doi.org/10.1007/s00262-008-0483-8.

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25

Zheng, Wenbiao, and Xinhua Chen. "Cloning and expression analysis of interferon-γ-inducible-lysosomal thiol reductase gene in large yellow croaker (Pseudosciaena crocea)." Molecular Immunology 43, no. 13 (May 2006): 2135–41. http://dx.doi.org/10.1016/j.molimm.2006.01.001.

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26

Haque, M. Azizul, Ping Li, Sheila K. Jackson, Hassane M. Zarour, John W. Hawes, Uyen T. Phan, Maja Maric, Peter Cresswell, and Janice S. Blum. "Absence of γ-Interferon–inducible Lysosomal Thiol Reductase in Melanomas Disrupts T Cell Recognition of Select Immunodominant Epitopes." Journal of Experimental Medicine 195, no. 10 (May 13, 2002): 1267–77. http://dx.doi.org/10.1084/jem.20011853.

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Long-lasting tumor immunity requires functional mobilization of CD8+ and CD4+ T lymphocytes. CD4+ T cell activation is enhanced by presentation of shed tumor antigens by professional antigen-presenting cells (APCs), coupled with display of similar antigenic epitopes by major histocompatibility complex class II on malignant cells. APCs readily processed and presented several self-antigens, yet T cell responses to these proteins were absent or reduced in the context of class II+ melanomas. T cell recognition of select exogenous and endogenous epitopes was dependent on tumor cell expression of γ-interferon–inducible lysosomal thiol reductase (GILT). The absence of GILT in melanomas altered antigen processing and the hierarchy of immunodominant epitope presentation. Mass spectral analysis also revealed GILT's ability to reduce cysteinylated epitopes. Such disparities in the profile of antigenic epitopes displayed by tumors and bystander APCs may contribute to tumor cell survival in the face of immunological defenses.

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27

Phan, U. T., R. L. Lackman, and P. Cresswell. "Role of the C-terminal propeptide in the activity and maturation of -interferon-inducible lysosomal thiol reductase (GILT)." Proceedings of the National Academy of Sciences 99, no. 19 (August 27, 2002): 12298–303. http://dx.doi.org/10.1073/pnas.182430499.

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28

Kongton, Kittima, Amornrat Phongdara, Moltira Tonganunt-Srithaworn, and Warapond Wanna. "Molecular cloning and expression analysis of the interferon-γ-inducible lysosomal thiol reductase gene from the shrimp Penaeus monodon." Molecular Biology Reports 38, no. 5 (November 26, 2010): 3463–70. http://dx.doi.org/10.1007/s11033-010-0456-9.

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29

Pang, Zan, Yao Zhang, and Liqin Liu. "Identification and functional characterization of interferon-γ-inducible lysosomal thiol reductase (GILT) gene in common Chinese cuttlefish Sepiella japonica." Fish & Shellfish Immunology 86 (March 2019): 627–34. http://dx.doi.org/10.1016/j.fsi.2018.12.004.

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30

Cui, Xian-wei, Wen Xiao, Zhen Ke, Xia Liu, Xing-zhou Xu, and Shuang-quan Zhang. "Cloning and expression analysis of interferon-γ-inducible-lysosomal thiol reductase gene in South African clawed frog (Xenopus laevis)." International Immunopharmacology 11, no. 12 (December 2011): 2091–97. http://dx.doi.org/10.1016/j.intimp.2011.09.001.

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31

Dan, Wen-Bing, Fang Ren, Chao Zhang, and Shuang-Quan Zhang. "Molecular cloning and expression analysis of interferon-γ-inducible-lysosomal thiol reductase gene in orange-spotted grouper, Epinephelus coioides." Fish & Shellfish Immunology 23, no. 6 (December 2007): 1315–23. http://dx.doi.org/10.1016/j.fsi.2007.07.005.

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32

Zhang, Dianchang, Dequan Pan, Shuge Cui, Tianfeng Su, Lihua Qiu, Caiyan Zhu, and Shigui Jiang. "Molecular characterization and expression analysis of interferon-γ-inducible lysosomal thiol reductase (GILT) gene from pearl oyster Pinctada fucata." Developmental & Comparative Immunology 34, no. 9 (September 2010): 969–76. http://dx.doi.org/10.1016/j.dci.2010.04.005.

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33

Fu, Jianping, Shannan Chen, Xin Zhao, Zhang Luo, Pengfei Zou, and Yi Liu. "Identification and characterization of the interferon-γ-inducible lysosomal thiol reductase gene in Chinese soft-shelled turtle, Pelodiscus sinensis." Developmental & Comparative Immunology 90 (January 2019): 55–59. http://dx.doi.org/10.1016/j.dci.2018.08.019.

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34

Yang, Lin, Xiang Cao, Xuemei Ji, Hongzhen Liu, Haitao Wu, Wei Gu, and Shuangquan Zhang. "Molecular structure, tissue distribution and functional characterization of interferon-γ-inducible lysosomal thiol reductase (GILT) gene in chicken (Gallus gallus)." Veterinary Immunology and Immunopathology 153, no. 1-2 (May 2013): 140–45. http://dx.doi.org/10.1016/j.vetimm.2013.01.011.

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35

Song, Jinyun, Hongzhen Liu, Lei Ma, Li Ma, Cuixiang Gao, and Shuangquan Zhang. "Molecular cloning, expression and functional characterization of interferon-γ-inducible lysosomal thiol reductase (GILT) gene from mandarin fish (Siniperca chuatsi)." Fish & Shellfish Immunology 38, no. 2 (June 2014): 275–81. http://dx.doi.org/10.1016/j.fsi.2014.03.021.

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36

Honey, Karen, Meghan Duff, Courtney Beers, William H. Brissette, Eileen A. Elliott, Christoph Peters, Maja Maric, Peter Cresswell, and Alexander Rudensky. "Cathepsin S Regulates the Expression of Cathepsin L and the Turnover of γ-Interferon-inducible Lysosomal Thiol Reductase in B Lymphocytes." Journal of Biological Chemistry 276, no. 25 (April 16, 2001): 22573–78. http://dx.doi.org/10.1074/jbc.m101851200.

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37

Li, Jian Feng, Jian Li, Zhi Guo Wang, Hong Zhen Liu, You Long Zhao, Jin Xi Zhang, Shuang Quan Zhang, and Jun Ping Liu. "Identification of interferon-γ-inducible-lysosomal thiol reductase (GILT) gene in goldfish (Carassius auratus) and its immune response to LPS challenge." Fish & Shellfish Immunology 42, no. 2 (February 2015): 465–72. http://dx.doi.org/10.1016/j.fsi.2014.11.032.

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38

Liu, Meng, Hongxin Ai, Wen Xiao, Yuefen Shen, Yang Shen, Xianwei Cui, and Shuangquan Zhang. "Identification of interferon-γ-inducible-lysosomal thiol reductase (GILT) gene from Mefugu (Takifugu obscures) and its immune response to LPS challenge." Developmental & Comparative Immunology 41, no. 2 (October 2013): 120–27. http://dx.doi.org/10.1016/j.dci.2013.04.023.

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39

De Zoysa, Mahanama, and Jehee Lee. "Molecular cloning and expression analysis of interferon-γ inducible lysosomal thiol reductase (GILT)-like cDNA from disk abalone (Haliotis discus discus)." Journal of Invertebrate Pathology 96, no. 3 (November 2007): 221–29. http://dx.doi.org/10.1016/j.jip.2007.05.009.

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40

Ai, Hong-xin, Zhen-zhen Zhang, Yue-fen Shen, Jia-xin Zhang, Xu-ming Zhou, Cui Min, Shan-yuan Zhu, and Shuang-quan Zhang. "Molecular structure, phylogenetic analysis, tissue distribution, and function characterization of interferon-γ-inducible lysosomal thiol reductase (GILT) gene in sheep (Ovis aries)." Veterinary Immunology and Immunopathology 140, no. 3-4 (April 2011): 329–34. http://dx.doi.org/10.1016/j.vetimm.2011.01.012.

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41

Wei, Zhou, Xu, Movahedi, Sun, Li, and Zhuge. "Identification and Characterization of an OSH1 Thiol Reductase from Populus trichocarpa." Cells 9, no. 1 (December 27, 2019): 76. http://dx.doi.org/10.3390/cells9010076.

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Interferon gamma-induced lysosomal thiol reductase (GILT) is abundantly expressed in antigen-presenting cells and participates in the treatment and presentation of antigens by major histocompatibility complex II. Also, GILT catalyzes the reduction of disulfide bonds, which plays an important role in cellular immunity. (1) Background: At present, the studies of GILT have mainly focused on animals. In plants, GILT homologous gene (Arabidopsis thaliana OSH1: AtOSH1) was discovered in the forward screen of mutants with compromised responses to sulphur nutrition. However, the complete properties and functions of poplar OSH1 are unclear. In addition, CdCl2 stress is swiftly engulfing the limited land resources on which humans depend, restricting agricultural production. (2) Methods: A prokaryotic expression system was used to produce recombinant PtOSH1 protein, and Western blotting was performed to identify its activity. In addition, a simplified version of the floral-dip method was used to transform A. thaliana. (3) Results: Here, we describe the identification and characterization of OSH1 from Populus trichocarpa. The deduced PtOSH1 sequence contained CQHGX2ECX2NX4C and CXXC motifs. The transcript level of PtOSH1 was increased by cadmium (Cd) treatment. In addition, recombinant PtOSH1 reduced disulfide bonds. A stress assay showed that PtOSH1-overexpressing (OE) A. thaliana lines had greater resistance to Cd than wild-type (WT) plants. Also, the activities of superoxide dismutase (SOD), peroxidase (POD), and catalase (CAT) in PtOSH1-OE plants were significantly higher than those in WT A. thaliana. These results indicate that PtOSH1 likely plays an important role in the response to Cd by regulating the reactive oxygen species (ROS)-scavenging system. (4) Conclusions: PtOSH1 catalyzes the reduction of disulfide bonds and behaves as a sulfhydryl reductase under acidic conditions. The overexpression of PtOSH1 in A. thaliana promoted root development, fresh weight, and dry weight; upregulated the expression levels of ROS scavenging-related genes; and improved the activity of antioxidant enzymes, enhancing plant tolerance to cadmium (Cd) stress. This study aimed to provide guidance that will facilitate future studies of the function of PtOSH1 in the response of plants to Cd stress.

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42

Merino, Kristen M., Geetha P. Bansal, and Nirbhay Kumar. "Reduced immunogenicity ofPlasmodium falciparumgamete surface antigen (Pfs48/45) in mice after disruption of disulphide bonds - evaluating effect of interferon-γ-inducible lysosomal thiol reductase." Immunology 148, no. 4 (June 29, 2016): 433–47. http://dx.doi.org/10.1111/imm.12621.

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43

You, Xiuling, Liu Liu, Xiuyu Li, Hejun Du, Dongsong Nie, Xingguo Zhang, Haibing Tong, Mingjiang Wu, Yitian Gao, and Zhiyong Liao. "Immune response of interferon-γ-inducible lysosomal thiol reductase (GILT) from Chinese sturgeon (Acipenser sinensis) to microbial invasion and its antioxdative activity in lipopolysaccharides-treated mammalian dentritic cells." Fish & Shellfish Immunology 72 (January 2018): 356–66. http://dx.doi.org/10.1016/j.fsi.2017.11.014.

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44

"Gamma-interferon-inducible lysosomal thiol reductase is upregulated in human melanoma." Journal of the American Academy of Dermatology 72, no. 5 (May 2015): AB30. http://dx.doi.org/10.1016/j.jaad.2015.02.132.

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45

"Correction: Absence of Gamma-Interferon-Inducible Lysosomal Thiol Reductase (GILT) Is Associated with Poor Disease-Free Survival in Breast Cancer Patients." PLOS ONE 10, no. 1 (January 28, 2015): e0117653. http://dx.doi.org/10.1371/journal.pone.0117653.

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46

Yang, Jing, Tyler R. Schleicher, Yuemei Dong, Hyun Bong Park, Jiangfeng Lan, Peter Cresswell, Jason Crawford, George Dimopoulos, and Erol Fikrig. "Disruption of mosGILT in Anopheles gambiae impairs ovarian development and Plasmodium infection." Journal of Experimental Medicine 217, no. 1 (October 28, 2019). http://dx.doi.org/10.1084/jem.20190682.

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Plasmodium infection in Anopheles is influenced by mosquito-derived factors. We previously showed that a protein in saliva from infected Anopheles, mosquito gamma-interferon–inducible lysosomal thiol reductase (mosGILT), inhibits the ability of sporozoites to traverse cells and readily establish infection of the vertebrate host. To determine whether mosGILT influences Plasmodium within the mosquito, we generated Anopheles gambiae mosquitoes carrying mosaic mutations in the mosGILT gene using CRISPR/CRISPR associated protein 9 (Cas9). Here, we show that female mosaic mosGILT mutant mosquitoes display defects in ovarian development and refractoriness to Plasmodium. Following infection by either Plasmodium berghei or Plasmodium falciparum, mutant mosquitoes have significantly reduced oocyst numbers as a result of increased thioester-containing protein 1 (TEP1)–dependent parasite killing. Expression of vitellogenin (Vg), the major yolk protein that can reduce the parasite-killing efficiency of TEP1, is severely impaired in mutant mosquitoes. MosGILT is a mosquito factor that is essential for ovarian development and indirectly protects both human and rodent Plasmodium species from mosquito immunity.

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