About: Purification and Characterisation of Immunoglobulins from the Australian Black Flying Fox (Pteropus alecto) Using Anti-Fab Affinity Chromatography Reveals the Low Abundance of IgA

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About: Purification and Characterisation of Immunoglobulins from the Australian Black Flying Fox (Pteropus alecto) Using Anti-Fab Affinity Chromatography Reveals the Low Abundance of IgA Goto Sponge NotDistinct Permalink

An Entity of Type : schema:ScholarlyArticle, within Data Space : wasabi.inria.fr associated with source document(s)

Attributes	Values
type	Academic Article research paper schema:ScholarlyArticle
isDefinedBy	Covid-on-the-Web dataset
has title	Purification and Characterisation of Immunoglobulins from the Australian Black Flying Fox (Pteropus alecto) Using Anti-Fab Affinity Chromatography Reveals the Low Abundance of IgA
Creator	Beddome, Gary Cowled, Christopher Di Rubbo, Antonio Huang, Jing Shiell, Brian Grimley, Samantha Baker, Michelle Michalski, Wojtek Peck, Grantley Wynne, James
Source	Medline; PMC
abstract	There is now an overwhelming body of evidence that implicates bats in the dissemination of a long list of emerging and re-emerging viral agents, often causing illnesses or death in both animals and humans. Despite this, there is a paucity of information regarding the immunological mechanisms by which bats coexist with highly pathogenic viruses. Immunoglobulins are major components of the adaptive immune system. Early studies found bats may have quantitatively lower antibody responses to model antigens compared to conventional laboratory animals. To further understand the antibody response of bats, the present study purified and characterised the major immunoglobulin classes from healthy black flying foxes, Pteropus alecto. We employed a novel strategy, where IgG was initially purified and used to generate anti-Fab specific antibodies. Immobilised anti-Fab specific antibodies were then used to capture other immunoglobulins from IgG depleted serum. While high quantities of IgM were successfully isolated from serum, IgA was not. Only trace quantities of IgA were detected in the serum by mass spectrometry. Immobilised ligands specific to IgA (Jacalin, Peptide M and staphylococcal superantigen-like protein) also failed to capture P. alecto IgA from serum. IgM was the second most abundant serum antibody after IgG. A survey of mucosal secretions found IgG was the dominant antibody class rather than IgA. Our study demonstrates healthy P. alecto bats have markedly less serum IgA than expected. Higher quantities of IgG in mucosal secretions may be compensation for this low abundance or lack of IgA. Knowledge and reagents developed within this study can be used in the future to examine class-specific antibody response within this important viral host.
has issue date	2013-01-07(xsd:dateTime)
bibo:doi	10.1371/journal.pone.0052930
bibo:pmid	23308125
has license	cc-by
sha1sum (hex)	bcd9208e1cff6a9d5e3af17745299ceea1479529
schema:url	https://doi.org/10.1371/journal.pone.0052930
resource representing a document's title	Purification and Characterisation of Immunoglobulins from the Australian Black Flying Fox (Pteropus alecto) Using Anti-Fab Affinity Chromatography Reveals the Low Abundance of IgA
has PubMed Central identifier	PMC3538733
has PubMed identifier	23308125
schema:publication	PLoS One
resource representing a document's body	covid:bcd9208e1cff6a9d5e3af17745299ceea1479529#body_text
is schema:about of	named entity 'ABUNDANCE' named entity 'antibodies' named entity 'strategy' named entity 'mucosal' named entity 'bats' named entity 'quantitatively' named entity 'host' named entity 'mass spectrometry' named entity 'P. alecto' named entity 'Fox' named entity 'Affinity' named entity 'OF EVIDENCE' named entity 'VIRAL' named entity 'DEPLETED' named entity 'STUDIES' named entity 'ANTIBODY RESPONSE' named entity 'PATHOGENIC' named entity 'HUMANS' named entity 'UNDERSTAND' named entity 'INITIALLY' named entity 'CONVENTIONAL' named entity 'REAGENTS' named entity 'MODEL' named entity 'SPECIFIC' named entity 'ANTIBODY' named entity 'BATS' named entity 'SPECIFIC ANTIBODY' named entity 'BLACK' named entity 'LIGANDS' named entity 'LACK' named entity 'IGM' named entity 'CLASS' named entity 'ANIMALS' named entity 'IGG' named entity 'SERUM' named entity 'FAILED' named entity 'NOVEL' named entity 'ANTIBODY CLASS' named entity 'RATHER' named entity 'MUCOSAL' named entity 'IMPORTANT' named entity 'INFORMATION' named entity 'DISSEMINATION' named entity 'USED' named entity 'FAB' named entity 'BODY' named entity 'COMPONENTS' named entity 'MECHANISMS' named entity 'STRATEGY' named entity 'IMMUNOLOGICAL' named entity 'RESPONSES' named entity 'CAUSING' named entity 'SECRETIONS' named entity 'IS A' named entity 'MAJOR' named entity 'HIGH' named entity 'LOWER' named entity 'ILLNESSES' named entity 'PRESENT' named entity 'CAPTURE' named entity 'EMPLOYED' named entity 'TO EXAMINE' named entity 'LABORATORY ANIMALS' named entity 'AFFINITY CHROMATOGRAPHY' named entity 'ISOLATED' named entity 'SECOND' named entity 'DOMINANT' named entity 'IMMUNOGLOBULINS' covid:arg/bcd9208e1cff6a9d5e3af17745299ceea1479529 named entity 'PEPTIDE M' named entity 'LONG' named entity 'IGA'

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