Targeting site-specific N-glycosylated B7H3 induces potent antitumor immunity

B7H3, an immune checkpoint molecule, is a highly N-glycosylated membrane protein. However, the key glycosylated asparagine residues that mediate the function of the B7H3 protein are still unclear. Here we identify that N-glycans attached to asparagine residues N91/309 and N104/322 are required for p...

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Published inNature communications Vol. 16; no. 1; pp. 3546 - 18
Main Authors Huang, Yun, Zhong, Wen-Qing, Yang, Xiao-Yu, Shan, Jia-Lu, Zhou, Ling, Li, Zhi-Ling, Guo, Yi-Qing, Zhang, Kai-Ming, Du, Tian, Zhang, Hai-Liang, Hu, Bing-Xin, Chen, Yu-Hong, Yang, Dong, Feng, Gong-Kan, Tang, Jun, Zhu, Xiao-Feng, Deng, Rong
Format Journal Article
LanguageEnglish
Published London Nature Publishing Group UK 14.04.2025
Nature Publishing Group
Nature Portfolio
Subjects
13/1
13/31
13/51
13/89
38/109
38/35
631/208/176
631/250/1619/554
631/67/1059
631/67/580
64/60
82/29
Animals
Antibodies, Monoclonal - immunology
Antibodies, Monoclonal - pharmacology
Asparagine
Asparagine - metabolism
B7 Antigens - genetics
B7 Antigens - immunology
B7 Antigens - metabolism
Biodegradation
Cell activation
Cell Line, Tumor
Cell Membrane - metabolism
Cell Proliferation
Cell surface
Cytotoxicity
Degradation
Endoplasmic reticulum
Endoplasmic Reticulum - metabolism
Female
Glycosylation
Golgi apparatus
Golgi Apparatus - metabolism
HEK293 Cells
Humanities and Social Sciences
Humans
Immune checkpoint
Immunity
Immunotherapy
Immunotherapy - methods
Internalization
Localization
Lymphocyte Activation
Lymphocytes
Lymphocytes T
Membranes
Mice
Mice, Inbred C57BL
Monoclonal antibodies
multidisciplinary
N-glycans
Neoplasms - immunology
Polysaccharides
Polysaccharides - metabolism
Protein Transport
Proteins
Residues
Science
Science (multidisciplinary)
T-Lymphocytes, Cytotoxic - immunology
Translocation
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Abstract B7H3, an immune checkpoint molecule, is a highly N-glycosylated membrane protein. However, the key glycosylated asparagine residues that mediate the function of the B7H3 protein are still unclear. Here we identify that N-glycans attached to asparagine residues N91/309 and N104/322 are required for proper B7H3 localization on the cell surface membrane. We demonstrate that mutations in these two pairs of N-glycosylation sites induce ER accumulation of B7H3 by blocking its ER-to-Golgi translocation and subsequently promote its degradation via the endoplasmic reticulum-associated protein degradation pathway. Additional evidence suggests that N-glycosylation at N91/309 and N104/322 of B7H3 is essential for its inhibition of T-cell proliferation and activation. More importantly, a monoclonal antibody, Ab-82, preferentially targeting B7H3 glycosylated at N91/309 and N104/322 is developed, which exhibits the ability to elicit cytotoxic T lymphocyte-mediated antitumor immunity via B7H3 internalization. Together, these findings offer a rationale for targeting glycosylated B7H3 as a potential strategy for immunotherapy. Glycosylated asparagine residues that mediate the function of the B7H3 protein are unclear. Here the authors identify the important N-glycosylation sites for B7H3 cell surface localization and T cell inhibition, followed by the development of N91/309 and N104/322 preferentially targeting monoclonal antibody manifesting enhanced antitumor immunity.
AbstractList B7H3, an immune checkpoint molecule, is a highly N-glycosylated membrane protein. However, the key glycosylated asparagine residues that mediate the function of the B7H3 protein are still unclear. Here we identify that N-glycans attached to asparagine residues N91/309 and N104/322 are required for proper B7H3 localization on the cell surface membrane. We demonstrate that mutations in these two pairs of N-glycosylation sites induce ER accumulation of B7H3 by blocking its ER-to-Golgi translocation and subsequently promote its degradation via the endoplasmic reticulum-associated protein degradation pathway. Additional evidence suggests that N-glycosylation at N91/309 and N104/322 of B7H3 is essential for its inhibition of T-cell proliferation and activation. More importantly, a monoclonal antibody, Ab-82, preferentially targeting B7H3 glycosylated at N91/309 and N104/322 is developed, which exhibits the ability to elicit cytotoxic T lymphocyte-mediated antitumor immunity via B7H3 internalization. Together, these findings offer a rationale for targeting glycosylated B7H3 as a potential strategy for immunotherapy.B7H3, an immune checkpoint molecule, is a highly N-glycosylated membrane protein. However, the key glycosylated asparagine residues that mediate the function of the B7H3 protein are still unclear. Here we identify that N-glycans attached to asparagine residues N91/309 and N104/322 are required for proper B7H3 localization on the cell surface membrane. We demonstrate that mutations in these two pairs of N-glycosylation sites induce ER accumulation of B7H3 by blocking its ER-to-Golgi translocation and subsequently promote its degradation via the endoplasmic reticulum-associated protein degradation pathway. Additional evidence suggests that N-glycosylation at N91/309 and N104/322 of B7H3 is essential for its inhibition of T-cell proliferation and activation. More importantly, a monoclonal antibody, Ab-82, preferentially targeting B7H3 glycosylated at N91/309 and N104/322 is developed, which exhibits the ability to elicit cytotoxic T lymphocyte-mediated antitumor immunity via B7H3 internalization. Together, these findings offer a rationale for targeting glycosylated B7H3 as a potential strategy for immunotherapy.
B7H3, an immune checkpoint molecule, is a highly N-glycosylated membrane protein. However, the key glycosylated asparagine residues that mediate the function of the B7H3 protein are still unclear. Here we identify that N-glycans attached to asparagine residues N91/309 and N104/322 are required for proper B7H3 localization on the cell surface membrane. We demonstrate that mutations in these two pairs of N-glycosylation sites induce ER accumulation of B7H3 by blocking its ER-to-Golgi translocation and subsequently promote its degradation via the endoplasmic reticulum-associated protein degradation pathway. Additional evidence suggests that N-glycosylation at N91/309 and N104/322 of B7H3 is essential for its inhibition of T-cell proliferation and activation. More importantly, a monoclonal antibody, Ab-82, preferentially targeting B7H3 glycosylated at N91/309 and N104/322 is developed, which exhibits the ability to elicit cytotoxic T lymphocyte-mediated antitumor immunity via B7H3 internalization. Together, these findings offer a rationale for targeting glycosylated B7H3 as a potential strategy for immunotherapy. Glycosylated asparagine residues that mediate the function of the B7H3 protein are unclear. Here the authors identify the important N-glycosylation sites for B7H3 cell surface localization and T cell inhibition, followed by the development of N91/309 and N104/322 preferentially targeting monoclonal antibody manifesting enhanced antitumor immunity.
Abstract B7H3, an immune checkpoint molecule, is a highly N-glycosylated membrane protein. However, the key glycosylated asparagine residues that mediate the function of the B7H3 protein are still unclear. Here we identify that N-glycans attached to asparagine residues N91/309 and N104/322 are required for proper B7H3 localization on the cell surface membrane. We demonstrate that mutations in these two pairs of N-glycosylation sites induce ER accumulation of B7H3 by blocking its ER-to-Golgi translocation and subsequently promote its degradation via the endoplasmic reticulum-associated protein degradation pathway. Additional evidence suggests that N-glycosylation at N91/309 and N104/322 of B7H3 is essential for its inhibition of T-cell proliferation and activation. More importantly, a monoclonal antibody, Ab-82, preferentially targeting B7H3 glycosylated at N91/309 and N104/322 is developed, which exhibits the ability to elicit cytotoxic T lymphocyte-mediated antitumor immunity via B7H3 internalization. Together, these findings offer a rationale for targeting glycosylated B7H3 as a potential strategy for immunotherapy.
B7H3, an immune checkpoint molecule, is a highly N-glycosylated membrane protein. However, the key glycosylated asparagine residues that mediate the function of the B7H3 protein are still unclear. Here we identify that N-glycans attached to asparagine residues N91/309 and N104/322 are required for proper B7H3 localization on the cell surface membrane. We demonstrate that mutations in these two pairs of N-glycosylation sites induce ER accumulation of B7H3 by blocking its ER-to-Golgi translocation and subsequently promote its degradation via the endoplasmic reticulum-associated protein degradation pathway. Additional evidence suggests that N-glycosylation at N91/309 and N104/322 of B7H3 is essential for its inhibition of T-cell proliferation and activation. More importantly, a monoclonal antibody, Ab-82, preferentially targeting B7H3 glycosylated at N91/309 and N104/322 is developed, which exhibits the ability to elicit cytotoxic T lymphocyte-mediated antitumor immunity via B7H3 internalization. Together, these findings offer a rationale for targeting glycosylated B7H3 as a potential strategy for immunotherapy.Glycosylated asparagine residues that mediate the function of the B7H3 protein are unclear. Here the authors identify the important N-glycosylation sites for B7H3 cell surface localization and T cell inhibition, followed by the development of N91/309 and N104/322 preferentially targeting monoclonal antibody manifesting enhanced antitumor immunity.
B7H3, an immune checkpoint molecule, is a highly N-glycosylated membrane protein. However, the key glycosylated asparagine residues that mediate the function of the B7H3 protein are still unclear. Here we identify that N-glycans attached to asparagine residues N91/309 and N104/322 are required for proper B7H3 localization on the cell surface membrane. We demonstrate that mutations in these two pairs of N-glycosylation sites induce ER accumulation of B7H3 by blocking its ER-to-Golgi translocation and subsequently promote its degradation via the endoplasmic reticulum-associated protein degradation pathway. Additional evidence suggests that N-glycosylation at N91/309 and N104/322 of B7H3 is essential for its inhibition of T-cell proliferation and activation. More importantly, a monoclonal antibody, Ab-82, preferentially targeting B7H3 glycosylated at N91/309 and N104/322 is developed, which exhibits the ability to elicit cytotoxic T lymphocyte-mediated antitumor immunity via B7H3 internalization. Together, these findings offer a rationale for targeting glycosylated B7H3 as a potential strategy for immunotherapy.
ArticleNumber 3546
Author Deng, Rong
Zhang, Hai-Liang
Feng, Gong-Kan
Zhang, Kai-Ming
Yang, Xiao-Yu
Zhong, Wen-Qing
Zhou, Ling
Hu, Bing-Xin
Yang, Dong
Li, Zhi-Ling
Du, Tian
Zhu, Xiao-Feng
Shan, Jia-Lu
Guo, Yi-Qing
Chen, Yu-Hong
Tang, Jun
Huang, Yun
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BackLink https://www.ncbi.nlm.nih.gov/pubmed/40229277$$D View this record in MEDLINE/PubMed
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Snippet B7H3, an immune checkpoint molecule, is a highly N-glycosylated membrane protein. However, the key glycosylated asparagine residues that mediate the function...
Abstract B7H3, an immune checkpoint molecule, is a highly N-glycosylated membrane protein. However, the key glycosylated asparagine residues that mediate the...
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13/31
13/51
13/89
38/109
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631/208/176
631/250/1619/554
631/67/1059
631/67/580
64/60
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Animals
Antibodies, Monoclonal - immunology
Antibodies, Monoclonal - pharmacology
Asparagine
Asparagine - metabolism
B7 Antigens - genetics
B7 Antigens - immunology
B7 Antigens - metabolism
Biodegradation
Cell activation
Cell Line, Tumor
Cell Membrane - metabolism
Cell Proliferation
Cell surface
Cytotoxicity
Degradation
Endoplasmic reticulum
Endoplasmic Reticulum - metabolism
Female
Glycosylation
Golgi apparatus
Golgi Apparatus - metabolism
HEK293 Cells
Humanities and Social Sciences
Humans
Immune checkpoint
Immunity
Immunotherapy
Immunotherapy - methods
Internalization
Localization
Lymphocyte Activation
Lymphocytes
Lymphocytes T
Membranes
Mice
Mice, Inbred C57BL
Monoclonal antibodies
multidisciplinary
N-glycans
Neoplasms - immunology
Polysaccharides
Polysaccharides - metabolism
Protein Transport
Proteins
Residues
Science
Science (multidisciplinary)
T-Lymphocytes, Cytotoxic - immunology
Translocation
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Title Targeting site-specific N-glycosylated B7H3 induces potent antitumor immunity
URI https://link.springer.com/article/10.1038/s41467-025-58740-3
https://www.ncbi.nlm.nih.gov/pubmed/40229277
https://www.proquest.com/docview/3190022274
https://www.proquest.com/docview/3190340476
https://pubmed.ncbi.nlm.nih.gov/PMC11997214
https://doaj.org/article/499634fe3b4a4a0598d27d5a31c80a36
Volume 16
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