The definition of five B lymphocyte alloantigens closely linked to BoLA class I antigens

1990 ◽  
Vol 21 (1) ◽  
pp. 69-76 ◽  
Author(s):  
J. T. MACKIE ◽  
M. J. STEAR
1989 ◽  
Vol 169 (1) ◽  
pp. 269-283 ◽  
Author(s):  
D Bessen ◽  
K F Jones ◽  
V A Fischetti

The antigenic relatedness of surface-exposed portions of M protein molecules derived from group A streptococcal isolates representing more than 50 distinct serotypes was examined. The data indicate that the majority of serotypes fall into two major classes. Class I M protein molecules share a surface-exposed, antigenic domain comprising the C repeat region defined for M6 protein. The C repeat region of M6 protein is located adjacent to the COOH-terminal side of the pepsin-susceptible site. In contrast, Class I M proteins display considerably less antigenic relatedness to the B repeat region of M6 protein, which lies immediately NH2-terminal to the pepsin site. Surface-exposed portions of Class II M proteins lack antigenic epitopes that define the Class I molecules. Studies in the 1970s demonstrated that M protein serotypes can be divided into two groups based on both immunoreactivity directed to an unknown surface antigen (termed M-associated protein) and production of serum opacity factor. These two groups closely parallel our current definition of Class I and Class II serotypes. Both classes retain the antiphagocytic property characteristic of M protein, and Class II M proteins share some immunodeterminants with Class I M proteins, although the shared determinants do not appear to be exposed on the streptococcal surface. Nearly all streptococcal serotypes associated with outbreaks of acute rheumatic fever express M protein of a Class I serotype. Thus, the surface-exposed, conserved C repeat domain of Class I serotypes may be a virulence determinant for rheumatic fever.


1993 ◽  
Vol 36 (1) ◽  
pp. 52
Author(s):  
M. Drouet ◽  
L. Aussel ◽  
R. Fauchet

2015 ◽  
Vol 195 (9) ◽  
pp. 4085-4095 ◽  
Author(s):  
Celia R. Berkers ◽  
Annemieke de Jong ◽  
Karianne G. Schuurman ◽  
Carsten Linnemann ◽  
Hugo D. Meiring ◽  
...  

2008 ◽  
Vol 205 (3) ◽  
pp. 595-610 ◽  
Author(s):  
Marie-Hélène Fortier ◽  
Étienne Caron ◽  
Marie-Pierre Hardy ◽  
Grégory Voisin ◽  
Sébastien Lemieux ◽  
...  

Under steady-state conditions, major histocompatibility complex (MHC) I molecules are associated with self-peptides that are collectively referred to as the MHC class I peptide (MIP) repertoire. Very little is known about the genesis and molecular composition of the MIP repertoire. We developed a novel high-throughput mass spectrometry approach that yields an accurate definition of the nature and relative abundance of unlabeled peptides presented by MHC I molecules. We identified 189 and 196 MHC I–associated peptides from normal and neoplastic mouse thymocytes, respectively. By integrating our peptidomic data with global profiling of the transcriptome, we reached two conclusions. The MIP repertoire of primary mouse thymocytes is biased toward peptides derived from highly abundant transcripts and is enriched in peptides derived from cyclins/cyclin-dependent kinases and helicases. Furthermore, we found that ∼25% of MHC I–associated peptides were differentially expressed on normal versus neoplastic thymocytes. Approximately half of those peptides are derived from molecules directly implicated in neoplastic transformation (e.g., components of the PI3K–AKT–mTOR pathway). In most cases, overexpression of MHC I peptides on cancer cells entailed posttranscriptional mechanisms. Our results show that high-throughput analysis and sequencing of MHC I–associated peptides yields unique insights into the genesis of the MIP repertoire in normal and neoplastic cells.


Author(s):  
Olesia V. Kamozina ◽  

All groups under consideration are assumed to be finite. For a nonempty subclass of Ω of the class of all simple groups I and the partition ζ = {ζi | i ∈ I}, where ζi is a nonempty subclass of the class I, I = ∪i∈I ζi and ζi ∩ ζj = ø for all i ≠ j, ΩζR-function f and ΩζFR-function φ are introduced. The domain of these functions is the set Ωζ ∪ {Ω′}, where Ωζ = { Ω ∩ ζi | Ω ∩ ζi ≠ ø }, Ω′ = I \ Ω. The scope of these function values is the set of Fitting classes and the set of nonempty Fitting formations, respectively. The functions f and φ are used to determine the Ωζ-foliated Fitting class F = ΩζR(f, φ) = (G : OΩ(G) ∈ f(Ω′) and G'φ(Ω ∩ ζi) ∈ f(Ω ∩ ζi) for all Ω ∩ ζi ∈ Ωζ(G)) with Ωζ-satellite f and Ωζ-direction φ. The paper gives examples of Ωζ-foliated Fitting classes. Two types of Ωζ-foliated Fitting classes are defined: Ωζ-free and Ωζ-canonical Fitting classes. Their directions are indicated by φ0 and φ1 respectively. It is shown that each non-empty non-identity Fitting class is a Ωζ-free Fitting class for some non-empty class Ω ⊆ I and any partition ζ. A series of properties of Ωζ-foliated Fitting classes is obtained. In particular, the definition of internal Ωζ-satellite is given and it is shown that every Ωζ-foliated Fitting class has an internal Ωζ-satellite. For Ω = I, the concept of a ζ-foliated Fitting class is introduced. The connection conditions between Ωζ-foliated and Ωζ-foliated Fitting classes are shown.


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