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Mammalian allergens
Published in Richard F. Lockey, Dennis K. Ledford, Allergens and Allergen Immunotherapy, 2020
Tuomas Virtanen, Marja Rytkönen-Nissinen
Human cellular immune response to Rat n 1 has been examined (see Section 16.4.1.1). One study found that HLA-DR7 is positively associated and HLA-DR3 negatively associated with sensitization to rat urinary proteins [136].
Gastroenterology and hepatology
Published in Shibley Rahman, Avinash Sharma, A Complete MRCP(UK) Parts 1 and 2 Written Examination Revision Guide, 2018
Shibley Rahman, Avinash Sharma
Coeliac disease is caused by sensitivity to the protein gluten. Repeated exposure leads to villous atrophy which in turn causes malabsorption. Conditions associated with coeliac disease include dermatitis herpetiformis (a vesicular, pruritic skin eruption) and autoimmune disorders (type 1 diabetes mellitus and autoimmune hepatitis). It is strongly associated with HLA-DQ2 (95% of patients) and HLA-B8 (80%) as well as HLA-DR3 and HLA-DR7.
Genetics, immunology, and pathogenesis
Published in M. Alan Menter, Caitriona Ryan, Psoriasis, 2017
Arthur Kavanaugh, Tristan Boyd
Although HLA-B alleles seem to confer increased risk for articular manifestations, HLA-C alleles confer greater susceptibility to cutaneous manifestations: HLA-Cw6 is associated with early-onset skin psoriasis, with a more severe and extensive presentation, but appears to have less of an association with articular symptoms.10 In addition to influencing disease phenotype, certain HLA antigens confer increased risk for disease progression (e.g., HLA-B39 alone and HLA-B27 in the presence of HLA-DR7), whereas others may reduce the risk of disease progression (e.g., HLA-B22 may be protective).11 Other genes, such as the shared epitope HLA-DRB1, when found in linkage disequilibrium with the aforementioned alleles, confer a worse radiological outcome (i.e., more erosive disease in peripheral joints) in PsA.12
The small molecule antibody mimic SH7139 targets a family of HLA-DRs expressed by B-cell lymphomas and other solid cancers
Published in Journal of Drug Targeting, 2020
Rod Balhorn, Monique Cosman Balhorn, Karuppiah Balakrishnan, Robert B. Rebhun
In the IHC assays conducted in this study, SH7129 exhibited very strong binding to its target as evidenced by its detection on the surface of the PBMCs expressing certain HLA-DRs even after thirteen buffer washes and two incubations (Table 2 and Figures 2 and 4). These results are consistent with the affinity of SH7129 reported previously for HLA-DR10 expressing Raji lymphoma cells (Kd ∼ 23pM) [22]. Although SH7129 is only 1/60th the size of an antibody, its affinity for HLA-DR7, HLA-DR9, HLA-DR10, HLA-DR11, HLA-DR12, HLA-DR13, HLA-DR15 and HLA-DR16 is similar to the best therapeutic monoclonal antibodies, which typically bind to their antigens with nM to pM affinities [97]. The observed lack of staining of PBMCs expressing HLA-DR1, HLA-DR3, HLA-DR4, HLA-DR8 and HLA-DR14 is most likely due to sequence differences predominantly in Site 2 that prevent Dv binding and to changes in Site 3 that block Cb binding. SH7129 may still bind to these HLA-DRs, but its affinity may not be high enough to remain bound under the stringent washing conditions used in our IHC assay. A one thousand-fold reduction in SHAL affinity would be expected if the sequence or structural changes eliminated the ability of one ligand to bind to HLA-DR. Bidentate SHALs containing only two ligands typically bind to their target protein with affinities in the nanomolar range. Picomolar affinities have only been observed with tridentate SHALs containing three ligands or with bis-bidentate SHALs that bind bivalently to two neighbouring HLA-DRs [22].
Immunogenetic predisposing factors for mesial temporal lobe epilepsy with hippocampal sclerosis
Published in International Journal of Neuroscience, 2018
Bárbara Leal, João Chaves, Cláudia Carvalho, Andreia Bettencourt, Cláudia Brito, Daniela Boleixa, Joel Freitas, Sandra Brás, João Lopes, João Ramalheira, Paulo P. Costa, Berta Martins da Silva, António Martins da Silva
It has also been observed that HS patients have higher numbers of CD4 and CD8 T cells in brain tissue than controls [16]. Beach et al. demonstrated that HS patients have an increase in HLA-DR-immunoreactive microglia and in HLA-DR-immunoreactive perivascular cells compared with controls [17]. The human leukocyte antigen (HLA) system has been implicated in diverse epileptic entities, such as juvenile myoclonic epilepsy (JME) [18–21] and Lennox-Gastaut syndrome [22,23], suggesting a variable role of this system in epilepsy. Nevertheless, the information about HLA in focal epilepsies is scarce. Ozkara et al. described an association of HLA-DR4, HLA-DR7 and HLA-DQ2 alleles and DR4-DQ2, DR7-DQ2 haplotypes with MTLE-HS development in a Turkish population [24]. Recently, in a Brazilian population, a higher frequency of HLA-DRB1*1302 allele in MTLE-HS patients compared with controls was described, although without statistical significance [25].
Targeting gp100 and TRP-2 with a DNA vaccine: Incorporating T cell epitopes with a human IgG1 antibody induces potent T cell responses that are associated with favourable clinical outcome in a phase I/II trial
Published in OncoImmunology, 2018
Poulam M. Patel, Christian H. Ottensmeier, Clive Mulatero, Paul Lorigan, Ruth Plummer, Hardev Pandha, Somaia Elsheikh, Efthymios Hadjimichael, Naty Villasanti, Sally E. Adams, Michelle Cunnell, Rachael L. Metheringham, Victoria A. Brentville, Lee Machado, Ian Daniels, Mohamed Gijon, Drew Hannaman, Lindy G. Durrant
Correlation of HLA phenotype and T cell responses are shown in Table 3. Only one of the patients responding to the gp100 long peptide did not express any of the HLA-DR7/DR53/DQ6 alleles, but this could indicate a response to the nested CD8 epitope. Ten of 25 patients responding to the gp100 HLA-DR4 epitope did not express the HLA-DR4 allele suggesting that this epitope has a more promiscuous binding and is not just restricted to HLA-DR4. Indeed, the Immune Epitope Database and Analysis Resource (IEDB) (http://tools.iedb.org/mhcii/) predicts that this epitope will bind better to HLA-DQ4 than HLA-DR4 (supplementary Table 2).