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Classical Flt3L-dependent dendritic cells control immunity to protein vaccine
Anandasabapathy, Niroshana,Feder, Rachel,Mollah, Shamim,Tse, Sze-Wah,Longhi, Maria Paula,Mehandru, Saurabh,Matos, Ines,Cheong, Cheolho,Ruane, Darren,Brane, Lucas,Teixeira, Angela,Dobrin, Joseph,Mizeni The Rockefeller University Press 2014 The Journal of experimental medicine Vol.211 No.9
<P>DCs are critical for initiating immunity. The current paradigm in vaccine biology is that DCs migrating from peripheral tissue and classical lymphoid-resident DCs (cDCs) cooperate in the draining LNs to initiate priming and proliferation of T cells. Here, we observe subcutaneous immunity is Fms-like tyrosine kinase 3 ligand (Flt3L) dependent. Flt3L is rapidly secreted after immunization; Flt3 deletion reduces T cell responses by 50%. Flt3L enhances global T cell and humoral immunity as well as both the numbers and antigen capture capacity of migratory DCs (migDCs) and LN-resident cDCs. Surprisingly, however, we find immunity is controlled by cDCs and actively tempered in vivo by migDCs. Deletion of Langerin<SUP>+</SUP> DC or blockade of DC migration improves immunity. Consistent with an immune-regulatory role, transcriptomic analyses reveals different skin migDC subsets in both mouse and human cluster together, and share immune-suppressing gene expression and regulatory pathways. These data reveal that protective immunity to protein vaccines is controlled by Flt3L-dependent, LN-resident cDCs.</P>
이성도,정형복,임봉수,이제희,김유철,김효원,THANTHRIGETHIUNUWAN PRIYATHILAKA,W. D. Niroshana Wickramaarachchi,김세재,김신권 한국유전학회 2014 Genes & Genomics Vol.36 No.4
Arginine vasotocin (AVT) is a neurohypophysialhormone of non-mammal vertebrates functions in variousphysiological processes and homologous to mammalvasopressin. In this study, a full-length cDNA coding for aputative AVT precursor was isolated from flounder, Paralichthysolivaceus by rapid amplification of cDNA ends. Itwas 641 bp long, coding 153 amino acids, and consisted in69 bp long 50-untranslated region (UTR), 462 bp openreading frame and 110 bp 30-UTR. The putative amino acidsequence of flounder AVT was determined, and comparedwith other AVTs from different species. Also, 1,447 bp offlounder AVT gene, corresponding to the isolated cDNAregion with 2 introns within it, was isolated. Reverse transcriptionpolymerase chain reaction result showed thatflounder AVT was strongly expressed in the brain but not inthe any other tissues examined, confirming it is brain-specificgene. Expression profile of the AVT, together with arylalkylamineN-acetyltransferase, heat shock protein 70,interferon-stimulated gene 15 and natural resistance-associatedmacrophage protein genes were surveyed fromStreptococcus iniae infected flounders by real-time quantitativePCR. It revealed that flounder AVT is up-regulatedunder acute stress compared to the non-challenged control.
( Young Deuk Lee ),( Chul Hong Oh ),( Mahanama De Zoysa ),( Hyo Won Kim ),( Wickramaarachchige Don Niroshana Wickramaarachchi ),( Ilson Whang ),( Do Hyung Kang ),( Je Hee Lee ) 한국미생물 · 생명공학회 2013 Journal of microbiology and biotechnology Vol.23 No.7
An agar-degrading bacterium was isolated from red seaweed (Gelidium amansii) on a natural seawater agar plate, and identified as Saccharophagus sp. AG21. The β-agarase gene from Saccharophagus sp. AG21 (agy1) was screened by long and accurate (LA)-PCR. The predicted sequence has a 1,908 bp open reading frame encoding 636 amino acids (aa), and includes a glycosyl hydrolase family 16 (GH16) β-agarase module and two carbohydrate binding modules of family 6 (CBM6). The deduced aa sequence showed 93.7% and 84.9% similarity to β-agarase of Saccharophagus degradans and Microbulbifer agarilyticus, respectively. The mature agy1 was cloned and overexpressed as a His-tagged recombinant β-agarase (rAgy1) in Escherichia coli, and had a predicted molecular mass of 69 kDa and an isoelectric point of 4.5. rAgy1 showed optimum activity at 55oC and pH 7.6, and had a specific activity of 85 U/mg. The rAgy1 activity was enhanced by FeSO4 (40%), KCl (34%), and NaCl (34%), compared with the control. The newly identified rAgy1 is a β-agarase, which acts to degrade agarose to neoagarotetraose (NA4) and neoagarohexaose (NA6) and may be useful for applications in the cosmetics, food, bioethanol, and reagent industries.