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Role of Antigen Glycosylation in Mucin Binding by Monoclonal Antibodies

Award Number: R15CA242349
ORGANIZATION: NATIONAL CANCER INSTITUTE
OPDIV: NIH
AWARD CLASS: DISCRETIONARY
AWARD ACTIVITY TYPE: SCIENTIFIC/HEALTH RESEARCH (INCLUDES SURVEYS)
PERIOD OF PERFORMANCE START DATE: 09/01/2020
PERIOD OF PERFORMANCE END DATE: 08/31/2024

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Role of Antigen Glycosylation in Mucin Binding by Monoclonal Antibodies - PROJECT SUMMARY Immunotherapy has become one of the central pillars of cancer treatment. The deployment of antibody-based therapies has transformed the lives of thousands of patients. A molecular understanding of how antibodies interact with their targets is invaluable for the development of new successful antibody drugs and immunotherapy products. One of the most important targets for the discovery of new cancer immunotherapies is the mucin family of glycoproteins. Mucin proteins are frequently overexpressed and display altered abnormal glycosylation in several types of adenocarcimona. However, despite the importance of mucin proteins as immunotherapy targets, little is known regarding how antibodies bind these proteins. To address this gap in our knowledge, we propose using a panel of antibodies that bind the mucins MUC1 and MUC16 as models to understand molecular recognition of these important therapeutic targets. Preliminary studies in our lab have demonstrated that glycosylation of MUC1 influences the conformational dynamics of epitopes which in turn influence antibody binding. We will expand our understanding of this phenomenon using a combination of structural biology, computational modeling and binding studies on a panel of MUC1 specific antibodies. Specifically, we aim to determine the role of cancer associated mucin glycosylation in antibody recognition of MUC1 (AIM 1). Previously published results suggest that MUC16 antibodies bind non-linear epitopes localized within the tandem-repeat region of the protein. This region is heavily glycosylated, and the role of MUC16 glycosylation on antibody binding is unknown. Preliminary studies in our lab have determined that a humanized MUC16 antibody binds to an epitope with a SEA domain. Using several therapeutic antibody candidates as models, we propose to employ structural and binding studies to characterize the nature of non-linear MUC16 epitopes recognized by therapeutic antibodies (AIM 2).


Issue Date FY	Funding FY	Legal Entity Name	Legal Entity Address	Legal Entity City	Legal Entity State	Legal Entity Zip Code	Legal Entity COUNTY	Legal Entity COUNTRY	Assistance Listing	Award Code	Budget Year	Action Date	Action Type	Action Amount

Issue Date FY: 2025 ( Subtotal = -$77,338 )
2025	2020	CALIFORNIA STATE UNIVERSITY, FRESNO	5150 N MAPLE AVE	FRESNO	CA	93740	FRESNO	USA	Cancer Biology Research	000	1	1/7/2025	NEW	-$77,338
														Subtotal = -$77,338

Issue Date FY: 2023 ( Subtotal = $0 )
2023	2020	CALIFORNIA STATE UNIVERSITY, FRESNO	5150 N MAPLE AVE	FRESNO	CA	93740	FRESNO	USA	Cancer Biology Research	000	1	8/22/2023	NEW	$0
														Subtotal = $0

Issue Date FY: 2020 ( Subtotal = $414,854 )
2020	2020	CALIFORNIA STATE UNIVERSITY, FRESNO	5241 N MAPLE AVE	FRESNO	CA	93740	FRESNO	USA	Cancer Biology Research	000	1	8/5/2020	NEW	$414,854
														Subtotal = $414,854

Grand Total All Awards = $337,516

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Role of Antigen Glycosylation in Mucin Binding by Monoclonal Antibodies

Award Number: R15CA242349

ORGANIZATION: NATIONAL CANCER INSTITUTE

OPDIV: NIH

AWARD CLASS: DISCRETIONARY

AWARD ACTIVITY TYPE: SCIENTIFIC/HEALTH RESEARCH (INCLUDES SURVEYS)

PERIOD OF PERFORMANCE START DATE: 09/01/2020

PERIOD OF PERFORMANCE END DATE: 08/31/2024

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