Human milk IgGs contain various combinations of different antigen-binding sites resulting in multiple variants of their bispecificity.

In the classic paradigm, immunoglobulins represent products of clonal B cell populations, each producing antibodies (Abs) recognizing a single antigen. There is a common belief that IgGs in mammalian biological fluids are monovalent molecules having stable structures and two identical antigen-bindin...

Descripción completa

Guardado en:

Detalles Bibliográficos
Autores principales:	Sergey E Sedykh, Valentina N Buneva, Georgy A Nevinsky
Formato:	article
Lenguaje:	EN
Publicado:	Public Library of Science (PLoS) 2012
Materias:	Medicine R Science Q
Acceso en línea:	https://doaj.org/article/60c38ab029df4fd294ca342b6e8bdd88
Etiquetas:	Agregar Etiqueta Sin Etiquetas, Sea el primero en etiquetar este registro!

id	oai:doaj.org-article:60c38ab029df4fd294ca342b6e8bdd88
record_format	dspace
spelling	oai:doaj.org-article:60c38ab029df4fd294ca342b6e8bdd882021-11-18T07:08:56ZHuman milk IgGs contain various combinations of different antigen-binding sites resulting in multiple variants of their bispecificity.1932-620310.1371/journal.pone.0042942https://doaj.org/article/60c38ab029df4fd294ca342b6e8bdd882012-01-01T00:00:00Zhttps://www.ncbi.nlm.nih.gov/pmc/articles/pmid/22912765/?tool=EBIhttps://doaj.org/toc/1932-6203In the classic paradigm, immunoglobulins represent products of clonal B cell populations, each producing antibodies (Abs) recognizing a single antigen. There is a common belief that IgGs in mammalian biological fluids are monovalent molecules having stable structures and two identical antigen-binding sites. However, human milk IgGs to different antigens undergo extensive half-molecule exchange. In the IgGs pool, only 33 ± 5% and 13 ± 5% of Abs contained light chains exclusively of kappa- or lambda-type, respectively, while 54 ± 10% of the IgGs contained both kappa- and lambda- light chains. All Ab preparations contained different amounts of IgGs of all four subclasses. Interestingly, lambda-IgGs contained an increased amount of IgG2 (87%) and only 3-6% of each of IgG1, IgG3, and IgG4, while kappa-IgGs consisted of comparable (17-32%) amounts of all IgG subtypes. Chimeric kappa-lambda-IgGs consisted of ~74% IgG1, ~16% IgG2, ~5% IgG3 and ~5% IgG4. As the result of the exchange, all IgG fractions eluted from several specific affinity sorbents under the conditions destroying strong immunocomplexes demonstrated high catalytic activities in hydrolysis of ATP, DNA, oligosaccharides, phosphorylation of proteins, lipids, and oligosaccharides. In vitro, an addition of reduced glutathione and milk plasma to two IgG fractions with different affinity for DNA-cellulose led to a transition of 25-60% of Ab of one fraction to the other fraction. Our data are indicative of the possibility of half-molecule exchange between milk IgGs of various subclasses, raised against different antigens (including abzymes), which explains the polyspecificity and cross-reactivity of these IgGs.Sergey E SedykhValentina N BunevaGeorgy A NevinskyPublic Library of Science (PLoS)articleMedicineRScienceQENPLoS ONE, Vol 7, Iss 8, p e42942 (2012)
institution	DOAJ
collection	DOAJ
language	EN
topic	Medicine R Science Q
spellingShingle	Medicine R Science Q Sergey E Sedykh Valentina N Buneva Georgy A Nevinsky Human milk IgGs contain various combinations of different antigen-binding sites resulting in multiple variants of their bispecificity.
description	In the classic paradigm, immunoglobulins represent products of clonal B cell populations, each producing antibodies (Abs) recognizing a single antigen. There is a common belief that IgGs in mammalian biological fluids are monovalent molecules having stable structures and two identical antigen-binding sites. However, human milk IgGs to different antigens undergo extensive half-molecule exchange. In the IgGs pool, only 33 ± 5% and 13 ± 5% of Abs contained light chains exclusively of kappa- or lambda-type, respectively, while 54 ± 10% of the IgGs contained both kappa- and lambda- light chains. All Ab preparations contained different amounts of IgGs of all four subclasses. Interestingly, lambda-IgGs contained an increased amount of IgG2 (87%) and only 3-6% of each of IgG1, IgG3, and IgG4, while kappa-IgGs consisted of comparable (17-32%) amounts of all IgG subtypes. Chimeric kappa-lambda-IgGs consisted of ~74% IgG1, ~16% IgG2, ~5% IgG3 and ~5% IgG4. As the result of the exchange, all IgG fractions eluted from several specific affinity sorbents under the conditions destroying strong immunocomplexes demonstrated high catalytic activities in hydrolysis of ATP, DNA, oligosaccharides, phosphorylation of proteins, lipids, and oligosaccharides. In vitro, an addition of reduced glutathione and milk plasma to two IgG fractions with different affinity for DNA-cellulose led to a transition of 25-60% of Ab of one fraction to the other fraction. Our data are indicative of the possibility of half-molecule exchange between milk IgGs of various subclasses, raised against different antigens (including abzymes), which explains the polyspecificity and cross-reactivity of these IgGs.
format	article
author	Sergey E Sedykh Valentina N Buneva Georgy A Nevinsky
author_facet	Sergey E Sedykh Valentina N Buneva Georgy A Nevinsky
author_sort	Sergey E Sedykh
title	Human milk IgGs contain various combinations of different antigen-binding sites resulting in multiple variants of their bispecificity.
title_short	Human milk IgGs contain various combinations of different antigen-binding sites resulting in multiple variants of their bispecificity.
title_full	Human milk IgGs contain various combinations of different antigen-binding sites resulting in multiple variants of their bispecificity.
title_fullStr	Human milk IgGs contain various combinations of different antigen-binding sites resulting in multiple variants of their bispecificity.
title_full_unstemmed	Human milk IgGs contain various combinations of different antigen-binding sites resulting in multiple variants of their bispecificity.
title_sort	human milk iggs contain various combinations of different antigen-binding sites resulting in multiple variants of their bispecificity.
publisher	Public Library of Science (PLoS)
publishDate	2012
url	https://doaj.org/article/60c38ab029df4fd294ca342b6e8bdd88
work_keys_str_mv	AT sergeyesedykh humanmilkiggscontainvariouscombinationsofdifferentantigenbindingsitesresultinginmultiplevariantsoftheirbispecificity AT valentinanbuneva humanmilkiggscontainvariouscombinationsofdifferentantigenbindingsitesresultinginmultiplevariantsoftheirbispecificity AT georgyanevinsky humanmilkiggscontainvariouscombinationsofdifferentantigenbindingsitesresultinginmultiplevariantsoftheirbispecificity
_version_	1718423854543536128

Human milk IgGs contain various combinations of different antigen-binding sites resulting in multiple variants of their bispecificity.

Ejemplares similares