1.To demonstrate the change in peripheral blood T lymphocyte subgroups and cytokines of Behet′s syndrome
Shulin SONG ; Dongmin BI ; Dongbao ZHAO ; Xinghai HAN
Chinese Journal of Rheumatology 2003;0(07):-
Objective To demonstrate the change in peripheral blood T lymphocyte subgroup and cytokines of Beh?et′s disease (BD). Methods T lymphocyte subgroup was detected by flow cytometry and serum interleukin (IL)-8, sIL-2R, IL-1?, IL-2, IL-6 and TNF-? were assayed by RIA. Results CD4, CD4/CD8, NK of BD decreased evidently and CD8 incrdased. Serum IL-8, sIL-2R increased compared to normal controls. Change of IL-2, IL-6, tumor necrosing factor (TNF)-? , IL-1? showed no statistical significance compared to normal group. Conclusion Change in peripheral blood T lymphocyte subgroup and serum IL-8, sIL-2R can be one of the activity index of BD.
2.Identification of determinants that mediate binding between Tembusu virus and the cellular receptor heat shock protein A9
Dongmin ZHAO ; Qingtao LIU ; Xinmei HUANG ; Huili WANG ; Kaikai HAN ; Jing YANG ; Keran BI ; Yuzhuo LIU ; Lijiao ZHANG ; Yin LI
Journal of Veterinary Science 2018;19(4):528-535
Heat shock protein A9 (HSPA9), a member of the heat shock protein family, is a putative receptor for Tembusu virus (TMUV). By using Western blot and co-immunoprecipitation assays, E protein domains I and II were identified as the functional domains that facilitate HSPA9 binding. Twenty-five overlapping peptides covering domain I and domain II sequences were synthesized and analyzed by using an HSPA9 binding assay. Two peptides showed the capability of binding to HSPA9. Dot blot assay of truncated peptides indicated that amino acid residues 19 to 22 and 245 to 252 of E protein constitute the minimal motifs required for TMUV binding to HSPA9. Importantly, peptides harboring those two minimal motifs could effectively inhibit TMUV infection. Our results provide insight into TMUV-receptor interaction, thereby creating opportunities for elucidating the mechanism of TMUV entry.
Blotting, Western
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Heat-Shock Proteins
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Hot Temperature
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Humans
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Immunoprecipitation
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Peptides
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Protein Structure, Tertiary