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Discover how PEPperPRINT Peptide Microarray products have been used in different fields of research.

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Antigenic characteristics of glycosylated protein 3 of highly pathogenic porcine reproductive and respiratory syndrome virus

Wang, Xinglong; Dang, Ruyi; Liu, Wenkai; Yang, Zengqi; Du, Enqi; Zhang, Shuxia
Virus Research.
Aug 2014
10.1016/j.virusres.2014.04.016
Highly pathogenic (HP)-porcine reproductive and respiratory syndrome virus (PRRSV) emerged in 2006 and has now become a global threat to pig farms. Despite extensive characterization of HP-PRRSV proteins by direct analysis and comparison with typical PRRSV, immune recognition remain poorly understood. Glycosylated protein 3 (GP3) has an important function in inducing protective immune response. To analyze the antigenic character of HP-PRRSV GP3, a total of 217 peptides were printed on a chip and used to react with HP-PRRSV specific serum. The reactions of these peptides to HP-PRRSV specific pig serum were scanned and quantified using the software PepSlide® Analyzer by fluorescence intensity. The intensity plots showed various reactions in different parts of GP3. The highest reaction intensity value reached 29,184.5 with the peptide sequence of CSENDHDELGFMVPP. Conversely, 88 peptides showed no reaction with 0 florescence intensity. A further analysis based on the result of the peptide microarray revealed an antigen reaction active region (AR) from Y51 to S106 in GP3. The AR had four parts of variation that may be a significant mutation of the typical PRRSV to HP-PRRSV. Acquired data may be useful for understanding HP-PRRSV variation and its GP3 immune recognition.

Anti-ADAMTS13 IgG autoantibodies present in healthy individuals share linear epitopes with those in patients with thrombotic thrombocytopenic purpura

Grillberger, R.; Casina, V. C.; Turecek, P. L.; Zheng, X. L.; Rottensteiner, H.; Scheiflinger, F.
Haematologica.
Apr 2014
10.3324/haematol.2013.100685

Analysis of Autoantibodies to 3-Hydroxy-3-methylglutaryl-coenzyme A Reductase Using Different Technologies

Musset, Lucile; Miyara, Makoto; Benveniste, Olivier; Charuel, Jean-Luc; Shikhman, Alexander; Boyer, Olivier; Fowler, Richard; Mammen, Andrew; Phillips, Joe; Mahler, Michael
Journal of Immunology Research.
Mar 2014
10.1155/2014/405956
Diagnostic tests are needed to aid in the diagnosis of necrotizing myopathies associated with statin use. This study aimed to compare different technologies for the detection of anti-HMGCR antibodies and analyze the clinical phenotype and autoantibody profile of the patients. Twenty samples from myositis patients positive for anti-HMGCR antibodies using a research addressable laser bead assay and 20 negative controls were tested for autoantibodies to HMGCR: QUANTA Lite HMGCR ELISA and QUANTA Flash HMGCR CIA. All patients were also tested for antibodies to extractable nuclear antigens and myositis related antibodies. To verify the specificity of the ELISA, 824 controls were tested. All three assays showed qualitative agreements of 100% and levels of anti-HMGCR antibodies showed significant correlation: Spearman’s rho > 0.8. The mean age of the anti-HMGCR antibody positive patients was 54.4 years, 16/20 were females, and 18/20 had necrotizing myopathy (two patients were not diagnosed). Nine out of 20 anti-HMGCR positive patients were on statin. All patients with anti-HMGCR antibodies were negative for all other autoantibodies tested. Testing various controls showed high specificity (99.3%). Anti-HMGCR antibodies are not always associated with the use of statin and appear to be the exclusive autoantibody specificity in patients with statin associated myopathies.

Histatin 5 binds to Porphyromonas gingivalis hemagglutinin B (HagB) and alters HagB-induced chemokine responses

Borgwardt, Derek S.; Martin, Aaron D.; Van Hemert, Jonathan R.; Yang, Jianyi; Fischer, Carol L.; Recker, Erica N.; Nair, Prashant R.; Vidva, Robinson; Chandrashekaraiah, Shwetha; Progulske-Fox, Ann; Drake, David; Cavanaugh, Joseph E.; Vali, Shireen; Zhang, Yang; Brogden, Kim A.
Sci Rep.
Jan 2014
10.1038/srep03904
Histatins are human salivary gland peptides with anti-microbial and anti-inflammatory activities. In this study, we hypothesized that histatin 5 binds to Porphyromonas gingivalis hemagglutinin B (HagB) and attenuates HagB-induced chemokine responses in human myeloid dendritic cells. Histatin 5 bound to immobilized HagB in a surface plasmon resonance (SPR) spectroscopy-based biosensor system. SPR spectroscopy kinetic and equilibrium analyses, protein microarray studies and I-TASSER structural modeling studies all demonstrated two histatin 5 binding sites on HagB. One site had a stronger affinity with a KD1 of 1.9 μM and one site had a weaker affinity with a KD2 of 60.0 μM. Binding has biological implications and predictive modeling studies and exposure of dendritic cells both demonstrated that 20.0 μM histatin 5 attenuated (p < 0.05) 0.02 μM HagB-induced CCL3/MIP-1α, CCL4/MIP-1β and TNFα responses. Thus histatin 5 is capable of attenuating chemokine responses, which may help control oral inflammation.

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