Loading…

Biparatopic antibodies: therapeutic applications and prospects

Biparatopic antibodies (bpAbs) bind distinct, non-overlapping epitopes on an antigen. This unique binding mode enables new mechanisms of action beyond monospecific and bispecific antibodies (bsAbs) that can make bpAbs effective therapeutics for various indications, including oncology and infectious...

Full description

Saved in:
Bibliographic Details
Published in:mAbs 2024-12, Vol.16 (1), p.2310890
Main Authors: Niquille, David L., Fitzgerald, Kyle M., Gera, Nimish
Format: Article
Language:English
Subjects:
Citations: Items that this one cites
Online Access:Get full text
Tags: Add Tag
No Tags, Be the first to tag this record!
cited_by
cites cdi_FETCH-LOGICAL-c483t-3f2ff30aa4ac373d94f9ece8eb5ddcc5cf6f9f0cc0563725bf7d338904abca023
container_end_page
container_issue 1
container_start_page 2310890
container_title mAbs
container_volume 16
creator Niquille, David L.
Fitzgerald, Kyle M.
Gera, Nimish
description Biparatopic antibodies (bpAbs) bind distinct, non-overlapping epitopes on an antigen. This unique binding mode enables new mechanisms of action beyond monospecific and bispecific antibodies (bsAbs) that can make bpAbs effective therapeutics for various indications, including oncology and infectious diseases. Biparatopic binding can lead to superior affinity and specificity, promote antagonism, lock target conformation, and result in higher-order target clustering. Such antibody-target complexes can elicit strong agonism, increase immune effector function, or result in rapid target downregulation and lysosomal trafficking. These are not only attractive properties for therapeutic antibodies but are increasingly being explored for other modalities such as antibody-drug conjugates, T-cell engagers and chimeric antigen receptors. Recent advances in bpAb engineering have enabled the construction of ever more sophisticated formats that are starting to show promise in the clinic.
doi_str_mv 10.1080/19420862.2024.2310890
format article
fullrecord <record><control><sourceid>proquest_pubme</sourceid><recordid>TN_cdi_pubmedcentral_primary_oai_pubmedcentral_nih_gov_10936611</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><doaj_id>oai_doaj_org_article_cded80158e66447d85469dfb9b9c7945</doaj_id><sourcerecordid>2937705936</sourcerecordid><originalsourceid>FETCH-LOGICAL-c483t-3f2ff30aa4ac373d94f9ece8eb5ddcc5cf6f9f0cc0563725bf7d338904abca023</originalsourceid><addsrcrecordid>eNp9kUlvFDEQhVsIRKKQnwCaI5cZylu7zYEtYokUiQucrWoviaOetrE9Qfn3uJnJiFzwxdbzq6_Kfl33ksCGwABviOIUhp5uKFC-oayJCp50p4u-hkHC0-O5pyfdeSm3sCwJRMLz7oQNnCkhyGn37lNImLHGFMwK5xrGaIMrb1f1xmVMblcXPaUpGKwhzqWZ7CrlWJIztbzonnmcijs_7Gfdzy-ff1x8W199_3p58fFqbfjA6pp56j0DRI6GSWYV98oZN7hRWGuMML73yoMxIHomqRi9tIy1N3EcDQJlZ93lnmsj3uqUwxbzvY4Y9F8h5muNuY06OW2sswMQMbi-51zaQfBeWT-qURmpuGis93tW2o1bZ42ba8bpEfTxzRxu9HW80wQU63tCGuH1gZDjr50rVW9DMW6acHZxVzRVTEoQzd2sYm817ctKdv7Yh4BestQPWeolS33IstW9-nfIY9VDcs3wYW8Is495i79jnqyueD_F7DPOJhTN_t_jD7fZr3s</addsrcrecordid><sourcetype>Open Website</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>2937705936</pqid></control><display><type>article</type><title>Biparatopic antibodies: therapeutic applications and prospects</title><source>Taylor &amp; Francis</source><source>PubMed Central</source><creator>Niquille, David L. ; Fitzgerald, Kyle M. ; Gera, Nimish</creator><creatorcontrib>Niquille, David L. ; Fitzgerald, Kyle M. ; Gera, Nimish</creatorcontrib><description>Biparatopic antibodies (bpAbs) bind distinct, non-overlapping epitopes on an antigen. This unique binding mode enables new mechanisms of action beyond monospecific and bispecific antibodies (bsAbs) that can make bpAbs effective therapeutics for various indications, including oncology and infectious diseases. Biparatopic binding can lead to superior affinity and specificity, promote antagonism, lock target conformation, and result in higher-order target clustering. Such antibody-target complexes can elicit strong agonism, increase immune effector function, or result in rapid target downregulation and lysosomal trafficking. These are not only attractive properties for therapeutic antibodies but are increasingly being explored for other modalities such as antibody-drug conjugates, T-cell engagers and chimeric antigen receptors. Recent advances in bpAb engineering have enabled the construction of ever more sophisticated formats that are starting to show promise in the clinic.</description><identifier>ISSN: 1942-0862</identifier><identifier>ISSN: 1942-0870</identifier><identifier>EISSN: 1942-0870</identifier><identifier>DOI: 10.1080/19420862.2024.2310890</identifier><identifier>PMID: 38439551</identifier><language>eng</language><publisher>United States: Taylor &amp; Francis</publisher><subject>Antibodies, Bispecific - therapeutic use ; Antibody engineering ; antibody-drug conjugates ; biparatopic antibodies ; bispecific antibodies ; chimeric antigen receptors ; Epitopes ; Immunoconjugates ; infectious disease ; oncology ; Receptors, Chimeric Antigen ; Review ; T-cell engagers</subject><ispartof>mAbs, 2024-12, Vol.16 (1), p.2310890</ispartof><rights>2024 The Author(s). Published with license by Taylor &amp; Francis Group, LLC. 2024</rights><rights>2024 The Author(s). Published with license by Taylor &amp; Francis Group, LLC. 2024 The Author(s)</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><cites>FETCH-LOGICAL-c483t-3f2ff30aa4ac373d94f9ece8eb5ddcc5cf6f9f0cc0563725bf7d338904abca023</cites><orcidid>0009-0000-0603-770X ; 0000-0003-2453-9468 ; 0000-0002-2295-8434</orcidid></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC10936611/pdf/$$EPDF$$P50$$Gpubmedcentral$$Hfree_for_read</linktopdf><linktohtml>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC10936611/$$EHTML$$P50$$Gpubmedcentral$$Hfree_for_read</linktohtml><link.rule.ids>230,314,723,776,780,881,27481,27903,27904,53770,53772,59120,59121</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/38439551$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Niquille, David L.</creatorcontrib><creatorcontrib>Fitzgerald, Kyle M.</creatorcontrib><creatorcontrib>Gera, Nimish</creatorcontrib><title>Biparatopic antibodies: therapeutic applications and prospects</title><title>mAbs</title><addtitle>MAbs</addtitle><description>Biparatopic antibodies (bpAbs) bind distinct, non-overlapping epitopes on an antigen. This unique binding mode enables new mechanisms of action beyond monospecific and bispecific antibodies (bsAbs) that can make bpAbs effective therapeutics for various indications, including oncology and infectious diseases. Biparatopic binding can lead to superior affinity and specificity, promote antagonism, lock target conformation, and result in higher-order target clustering. Such antibody-target complexes can elicit strong agonism, increase immune effector function, or result in rapid target downregulation and lysosomal trafficking. These are not only attractive properties for therapeutic antibodies but are increasingly being explored for other modalities such as antibody-drug conjugates, T-cell engagers and chimeric antigen receptors. Recent advances in bpAb engineering have enabled the construction of ever more sophisticated formats that are starting to show promise in the clinic.</description><subject>Antibodies, Bispecific - therapeutic use</subject><subject>Antibody engineering</subject><subject>antibody-drug conjugates</subject><subject>biparatopic antibodies</subject><subject>bispecific antibodies</subject><subject>chimeric antigen receptors</subject><subject>Epitopes</subject><subject>Immunoconjugates</subject><subject>infectious disease</subject><subject>oncology</subject><subject>Receptors, Chimeric Antigen</subject><subject>Review</subject><subject>T-cell engagers</subject><issn>1942-0862</issn><issn>1942-0870</issn><issn>1942-0870</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2024</creationdate><recordtype>article</recordtype><sourceid>0YH</sourceid><sourceid>DOA</sourceid><recordid>eNp9kUlvFDEQhVsIRKKQnwCaI5cZylu7zYEtYokUiQucrWoviaOetrE9Qfn3uJnJiFzwxdbzq6_Kfl33ksCGwABviOIUhp5uKFC-oayJCp50p4u-hkHC0-O5pyfdeSm3sCwJRMLz7oQNnCkhyGn37lNImLHGFMwK5xrGaIMrb1f1xmVMblcXPaUpGKwhzqWZ7CrlWJIztbzonnmcijs_7Gfdzy-ff1x8W199_3p58fFqbfjA6pp56j0DRI6GSWYV98oZN7hRWGuMML73yoMxIHomqRi9tIy1N3EcDQJlZ93lnmsj3uqUwxbzvY4Y9F8h5muNuY06OW2sswMQMbi-51zaQfBeWT-qURmpuGis93tW2o1bZ42ba8bpEfTxzRxu9HW80wQU63tCGuH1gZDjr50rVW9DMW6acHZxVzRVTEoQzd2sYm817ctKdv7Yh4BestQPWeolS33IstW9-nfIY9VDcs3wYW8Is495i79jnqyueD_F7DPOJhTN_t_jD7fZr3s</recordid><startdate>20241231</startdate><enddate>20241231</enddate><creator>Niquille, David L.</creator><creator>Fitzgerald, Kyle M.</creator><creator>Gera, Nimish</creator><general>Taylor &amp; Francis</general><general>Taylor &amp; Francis Group</general><scope>0YH</scope><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7X8</scope><scope>5PM</scope><scope>DOA</scope><orcidid>https://orcid.org/0009-0000-0603-770X</orcidid><orcidid>https://orcid.org/0000-0003-2453-9468</orcidid><orcidid>https://orcid.org/0000-0002-2295-8434</orcidid></search><sort><creationdate>20241231</creationdate><title>Biparatopic antibodies: therapeutic applications and prospects</title><author>Niquille, David L. ; Fitzgerald, Kyle M. ; Gera, Nimish</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c483t-3f2ff30aa4ac373d94f9ece8eb5ddcc5cf6f9f0cc0563725bf7d338904abca023</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2024</creationdate><topic>Antibodies, Bispecific - therapeutic use</topic><topic>Antibody engineering</topic><topic>antibody-drug conjugates</topic><topic>biparatopic antibodies</topic><topic>bispecific antibodies</topic><topic>chimeric antigen receptors</topic><topic>Epitopes</topic><topic>Immunoconjugates</topic><topic>infectious disease</topic><topic>oncology</topic><topic>Receptors, Chimeric Antigen</topic><topic>Review</topic><topic>T-cell engagers</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Niquille, David L.</creatorcontrib><creatorcontrib>Fitzgerald, Kyle M.</creatorcontrib><creatorcontrib>Gera, Nimish</creatorcontrib><collection>Taylor &amp; Francis</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>MEDLINE - Academic</collection><collection>PubMed Central (Full Participant titles)</collection><collection>DOAJ Directory of Open Access Journals</collection><jtitle>mAbs</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Niquille, David L.</au><au>Fitzgerald, Kyle M.</au><au>Gera, Nimish</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Biparatopic antibodies: therapeutic applications and prospects</atitle><jtitle>mAbs</jtitle><addtitle>MAbs</addtitle><date>2024-12-31</date><risdate>2024</risdate><volume>16</volume><issue>1</issue><spage>2310890</spage><pages>2310890-</pages><issn>1942-0862</issn><issn>1942-0870</issn><eissn>1942-0870</eissn><abstract>Biparatopic antibodies (bpAbs) bind distinct, non-overlapping epitopes on an antigen. This unique binding mode enables new mechanisms of action beyond monospecific and bispecific antibodies (bsAbs) that can make bpAbs effective therapeutics for various indications, including oncology and infectious diseases. Biparatopic binding can lead to superior affinity and specificity, promote antagonism, lock target conformation, and result in higher-order target clustering. Such antibody-target complexes can elicit strong agonism, increase immune effector function, or result in rapid target downregulation and lysosomal trafficking. These are not only attractive properties for therapeutic antibodies but are increasingly being explored for other modalities such as antibody-drug conjugates, T-cell engagers and chimeric antigen receptors. Recent advances in bpAb engineering have enabled the construction of ever more sophisticated formats that are starting to show promise in the clinic.</abstract><cop>United States</cop><pub>Taylor &amp; Francis</pub><pmid>38439551</pmid><doi>10.1080/19420862.2024.2310890</doi><orcidid>https://orcid.org/0009-0000-0603-770X</orcidid><orcidid>https://orcid.org/0000-0003-2453-9468</orcidid><orcidid>https://orcid.org/0000-0002-2295-8434</orcidid><oa>free_for_read</oa></addata></record>
fulltext fulltext
identifier ISSN: 1942-0862
ispartof mAbs, 2024-12, Vol.16 (1), p.2310890
issn 1942-0862
1942-0870
1942-0870
language eng
recordid cdi_pubmedcentral_primary_oai_pubmedcentral_nih_gov_10936611
source Taylor & Francis; PubMed Central
subjects Antibodies, Bispecific - therapeutic use
Antibody engineering
antibody-drug conjugates
biparatopic antibodies
bispecific antibodies
chimeric antigen receptors
Epitopes
Immunoconjugates
infectious disease
oncology
Receptors, Chimeric Antigen
Review
T-cell engagers
title Biparatopic antibodies: therapeutic applications and prospects
url http://sfxeu10.hosted.exlibrisgroup.com/loughborough?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2025-01-21T17%3A08%3A00IST&url_ver=Z39.88-2004&url_ctx_fmt=infofi/fmt:kev:mtx:ctx&rfr_id=info:sid/primo.exlibrisgroup.com:primo3-Article-proquest_pubme&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.genre=article&rft.atitle=Biparatopic%20antibodies:%20therapeutic%20applications%20and%20prospects&rft.jtitle=mAbs&rft.au=Niquille,%20David%20L.&rft.date=2024-12-31&rft.volume=16&rft.issue=1&rft.spage=2310890&rft.pages=2310890-&rft.issn=1942-0862&rft.eissn=1942-0870&rft_id=info:doi/10.1080/19420862.2024.2310890&rft_dat=%3Cproquest_pubme%3E2937705936%3C/proquest_pubme%3E%3Cgrp_id%3Ecdi_FETCH-LOGICAL-c483t-3f2ff30aa4ac373d94f9ece8eb5ddcc5cf6f9f0cc0563725bf7d338904abca023%3C/grp_id%3E%3Coa%3E%3C/oa%3E%3Curl%3E%3C/url%3E&rft_id=info:oai/&rft_pqid=2937705936&rft_id=info:pmid/38439551&rfr_iscdi=true