Figure - PMC

Skip to main content

An official website of the United States government

Here's how you know

Here's how you know

Official websites use .gov
A .gov website belongs to an official government organization in the United States.

Secure .gov websites use HTTPS
A lock ( ) or https:// means you've safely connected to the .gov website. Share sensitive information only on official, secure websites.

View full-text article in PMC

. 2021 Jun 21;9(6):680. doi: 10.3390/vaccines9060680

Search in PMC
Search in PubMed
View in NLM Catalog
Add to search

© 2021 by the authors.

Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (https://creativecommons.org/licenses/by/4.0/).

PMC Copyright notice

HLA-I polyreactivity of IVIg. IVIg was tested on three kinds of SABs: (i) regular LABScreen bead set coated with an admixture of CCs and OCs, (ii) regular LABScreen bead set treated with a mild acid to convert OCs to CCs. The bead set was loaded with OCs. (iii) “iBeads” generated from regular LABScreen bead sets to enzymatically eliminate OCs, and therefore containing only CCs. The Luminex immunoassay with IVIg from GammaSTAN (A) and Octagam (B) confirmed the HLA-I polyreactivity of IVIg. Importantly, IVIG reacted with the monomeric variants on the acid-denatured SABs better than on iBeads. The density of IgG binding is illustrated by mean fluorescent intensity (MFI), as shown in different colors. The binding affinity of IVIg to monomeric variants was much higher than those recognizing the CC on ‘iBeads.’.

HLA-I polyreactivity of IVIg. IVIg was tested on three kinds of SABs: (i) regular LABScreen bead set coated with an admixture of CCs and OCs, (ii) regular LABScreen bead set treated with a mild acid to convert OCs to CCs. The bead set was loaded with OCs. (iii) “iBeads” generated from regular LABScreen bead sets to enzymatically eliminate OCs, and therefore containing only CCs. The Luminex immunoassay with IVIg from GammaSTAN (A) and Octagam (B) confirmed the HLA-I polyreactivity of IVIg. Importantly, IVIG reacted with the monomeric variants on the acid-denatured SABs better than on iBeads. The density of IgG binding is illustrated by mean fluorescent intensity (MFI), as shown in different colors. The binding affinity of IVIg to monomeric variants was much higher than those recognizing the CC on ‘iBeads.’.