Bacterial Modulation of Fc Effector Functions

Collin, Mattias; Kilian, Mogens

doi:10.1016/b978-0-12-394802-1.00018-2

Cited by 4 publications

(12 citation statements)

References 127 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Analogous shielding speculations had been made for cleaved IgAs (in those cases catalyzed by bacterial proteinases) in tissues and in the digestive tract. 21,40 Moreover, it has proven difficult to demonstrate hinge-cleaved IgGs in circulation – an observation consistent with retained, localized binding of these IgG derivatives.…”

Section: Direct Detection Of Cleaved Iggs In Situmentioning

confidence: 99%

“…IdeS is unique in its selectivity for human IgGs and, in addition to its reagent uses, has potential therapeutic applications for counteracting autoimmunity. 19,21,27,28 IdeS hydrolyzes bonds in the lower hinge of all four human IgG subclasses – but not those of other mammalian groups. The absence of extraneous proteinolysis largely avoids complicating side effects in the tumor microenvironment, making IdeS ideal for engineered tumor cell modeling studies.…”

Section: Introductionmentioning

confidence: 96%

“…19,20 In this regard, they are dissimilar from a group of bacterial proteinases that evolved a strict specificity for human IgA. 21 Also, IgG fragmentation with human and most bacterial proteinases has generally been found to be slower than with papain or pepsin. This difference largely explains the historical emphasis placed on the latter proteinases.…”

Section: Introductionmentioning

confidence: 99%

See 2 more Smart Citations

Proteinase-nicked IgGs: an unanticipated target for tumor immunotherapy

et al. 2018

View full text Add to dashboard Cite

The host immune system adopts multiple mechanisms involving antibodies to confront cancer cells. Accordingly, anti-tumor mAbs have become mainstays in cancer treatment. However, neither host immunity nor mAb therapies appear capable of controlling tumor growth in all cases. Structural instability of IgG was overlooked as a factor contributing to immunosuppression in the tumor microenvironment. Recently, physiological proteinases were identified that disable IgG immune effector functions. Evidence shows that these proteinases cause localized IgG impairment by selective cleavage of a single IgG peptide bond in the hinge-region. The recognition of IgG cleavage in the tumor microenvironment provides alternatives for tumor immunotherapy.

show abstract

Section: Direct Detection Of Cleaved Iggs In Situmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 96%

Section: Introductionmentioning

confidence: 99%

See 1 more Smart Citation

Proteinase-nicked IgGs: an unanticipated target for tumor immunotherapy

et al. 2018

View full text Add to dashboard Cite

show abstract

“…The significance of the host’s innate surveillance mechanisms for pathogen clearance is demonstrated by the diverse arsenal of virulence determinants and evasive strategies identified in many human-pathogenic bacteria capable of interfering with complement and, thereby, promoting immune evasion ( 7 , 8 ). Bacterial surface proteins capable of nonimmune immunoglobulin (Ig) binding are key players in immune evasion due to protection against complement attack, decreasing opsonization and phagocytosis, or both ( 15 – 17 ). Moreover, a second known function of proteins binding to Ig, without involving the antigen-binding site, is to act as B-cell or immunoglobulin superantigens ( 18 – 20 ).…”

Section: Introductionmentioning

confidence: 99%

The Retropepsin-Type Protease APRc as a Novel Ig-Binding Protein and Moonlighting Immune Evasion Factor ofRickettsia

Curto

Barro

Almeida³

et al. 2021

mBio

View full text Add to dashboard Cite

show abstract

“…The best known example of such a molecule is Protein A, which is utilized by Staphylococcus aureus to mis-orient IgG; however, microbes possessing a number of diverse alternative means of antibody-evasion exist (Collin and Killian, 2014). Enzymes such as IdeS and SpeB restrict the Fc domain by cleaving Abs in their hinge region, and a number of glycosidases with activity against IgG and IgA glycans have been identified.…”

Section: Introductionmentioning

confidence: 99%

Microscale purification of antigen-specific antibodies

Brown

Normandin

Osei-Owusu

et al. 2015

Journal of Immunological Methods

View full text Add to dashboard Cite

Glycosylation of the Fc domain is an important driver of antibody effector function. While assessment of antibody glycoform compositions observed across total plasma IgG has identified differences associated with a variety of clinical conditions, in many cases it is the glycosylation state of only antibodies against a specific antigen or set of antigens that may be of interest, for example, in defining the potential effector function of antibodies produced during disease or after vaccination. Historically, glycoprofiling such antigen-specific antibodies in clinical samples has been challenging due to their low prevalence, the high sample requirement for most methods of glycan determination, and the lack of high-throughput purification methods. New methods of glycoprofiling with lower sample requirements and higher throughput have motivated the development of microscale and automatable methods for purification of antigen-specific antibodies from polyclonal sources such as clinical serum samples. In this work, we present a robot-compatible 96-well plate-based method for purification of antigen-specific antibodies, suitable for such population level glycosylation screening. We demonstrate the utility of this method across multiple antibody sources, using both purified plasma IgG and plasma, and across multiple different antigen types, with enrichment factors greater than 1000-fold observed. Using an on-column IdeS protease treatment, we further describe staged release of Fc and Fab domains, allowing for glycoprofiling of each domain.

show abstract

Bacterial Modulation of Fc Effector Functions

Cited by 4 publications

References 127 publications

Proteinase-nicked IgGs: an unanticipated target for tumor immunotherapy

Proteinase-nicked IgGs: an unanticipated target for tumor immunotherapy

The Retropepsin-Type Protease APRc as a Novel Ig-Binding Protein and Moonlighting Immune Evasion Factor ofRickettsia

Microscale purification of antigen-specific antibodies

Contact Info

Product

Resources

About