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  • Khumthong, Rabuesak  (6)
  • 1
    Online Resource
    Online Resource
    The Company of Biologists ; 2008
    In:  Journal of Experimental Biology Vol. 211, No. 21 ( 2008-11-01), p. 3401-3408
    In: Journal of Experimental Biology, The Company of Biologists, Vol. 211, No. 21 ( 2008-11-01), p. 3401-3408
    Abstract: The organic anion transporting polypeptides (Oatps in rodents and other organism; OATPs in human) are Na+-independent transporters that shuttle a wide range of endogenous and xenobotic amphipathic compounds across plasma membranes. We previously discovered an Amblyomma americanumtick (Aam) Oatp cDNA among genes that were upregulated or induced in ticks that were stimulated to start feeding. In this study, we have characterized a 2860 bp full-length cDNA that encode a 724 amino acid putative protein. Bioinformatics and hydropathy analyses revealed that, in addition to the kazal-type serine proteinase inhibitor motif, AamOatp possess typical features that characterize the Oatp/OATP protein family, including 12 transmembrane (TM) domains, the consensus amino acid motif D-X-RW-(I,V)-GAWW-X-G-(F,L)-L and 11 consensus cysteine residues in the large extracellular domain between TM9 and TM10. AamOatp is constitutively and ubiquitously expressed, as determined by RT-PCR amplification of the transcript, in all organs of ticks that fed for 1–7 days. Analysis of the normalized transcript abundance revealed that from days 1 to 5 of feeding, AamOatp mRNA expression in the midgut (MG) was 60–80-fold higher than levels found in the salivary gland (SG), ovary (OV) and carcass(CA). By contrast, by day 7 of feeding, the AamOatp mRNA was 60–80-fold more strongly expressed in the OV than in the SG, MG and CA. These data strongly indicate that changing physiological needs during the tick feeding process influences transcriptional regulation of AamOatp. Our data also show that RNAi-mediated suppression of the AamOatp caused ticks to obtain smaller blood meals, which consequently resulted in ticks laying fewer eggs. The results are discussed in the context of AamOatp as a potential pharmacological or anti-tick vaccine target.
    Type of Medium: Online Resource
    ISSN: 1477-9145 , 0022-0949
    Language: English
    Publisher: The Company of Biologists
    Publication Date: 2008
    detail.hit.zdb_id: 1482461-9
    SSG: 12
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  • 2
    Online Resource
    Online Resource
    Springer Science and Business Media LLC ; 2007
    In:  Experimental and Applied Acarology Vol. 41, No. 4 ( 2007-04), p. 267-287
    In: Experimental and Applied Acarology, Springer Science and Business Media LLC, Vol. 41, No. 4 ( 2007-04), p. 267-287
    Type of Medium: Online Resource
    ISSN: 0168-8162 , 1572-9702
    Language: English
    Publisher: Springer Science and Business Media LLC
    Publication Date: 2007
    detail.hit.zdb_id: 1497718-7
    SSG: 12
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  • 3
    Online Resource
    Online Resource
    The Company of Biologists ; 2010
    In:  Journal of Experimental Biology Vol. 213, No. 7 ( 2010-04-01), p. 1153-1161
    In: Journal of Experimental Biology, The Company of Biologists, Vol. 213, No. 7 ( 2010-04-01), p. 1153-1161
    Abstract: The insulin-like growth factor (IGF) binding proteins (IGFBP) family is the regulatory arm of the IGF signaling system that control mitogenic and anabolic actions of IGF peptide hormones. This study describes cloning and biological characterization of three Amblyomma americanum (L.) (Aam) proteins that show amino-terminal sequence and secondary structure similarity to the IGFBP superfamily. The three molecules here provisionally identified as AamIGFBP-rP1 and short (S) and long (L) AamIGFBP-rP6 are expressed in multiple tick organs and are responsive to tick feeding activity with the former being upregulated and the latter being downregulated. We show that they regulate tick physiological functions that may be related to A. americanum tick feeding success as revealed by RNAi-mediated dual silencing of AamIGFBP-rP6S and AamIGFBP-rP6L or AamIGFBP-rP1 alone, which caused a reduction in blood meal size compared to the controls. Additionally, in the case of AamIGFBP-rP1 silencing, 47% of ticks died while attempting to feed and those that did survive and spontaneously detached from the host failed to lay eggs. Although AamIGFBP-rP6S and AamIGFBP-rP6L show overall identities of 49% and 59%, respectively, to Rhipicephalus microplus C protein, the identity level jumps to ~84% when the comparison is restricted to first 70 amino acids of the mature protein. Similarly, the AamIGFBP-rP1 mature protein is ~72%, 87%, 88% and 92% identical to that of Ixodes scapularis S, R. microplus, R. appendiculatus N and A. variegatum F, respectively. The observed across-tick-species conservation suggests that the three molecules (AamIGFBP-rP1, AamIGFBP-rP6S and AamIGFBP-rP6L) represent target for development of vaccines to protect animals against multiple tick species. The data are discussed with reference to advances in tick molecular biology and the potential of the three proteins as targets for immunizing animals against tick feeding.
    Type of Medium: Online Resource
    ISSN: 1477-9145 , 0022-0949
    Language: English
    Publisher: The Company of Biologists
    Publication Date: 2010
    detail.hit.zdb_id: 1482461-9
    SSG: 12
    Location Call Number Limitation Availability
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  • 4
    Online Resource
    Online Resource
    Springer Science and Business Media LLC ; 2009
    In:  BMC Genomics Vol. 10, No. 1 ( 2009), p. 217-
    In: BMC Genomics, Springer Science and Business Media LLC, Vol. 10, No. 1 ( 2009), p. 217-
    Type of Medium: Online Resource
    ISSN: 1471-2164
    Language: English
    Publisher: Springer Science and Business Media LLC
    Publication Date: 2009
    detail.hit.zdb_id: 2041499-7
    SSG: 12
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  • 5
    Online Resource
    Online Resource
    The Company of Biologists ; 2007
    In:  Journal of Experimental Biology Vol. 210, No. 18 ( 2007-09-15), p. 3188-3198
    In: Journal of Experimental Biology, The Company of Biologists, Vol. 210, No. 18 ( 2007-09-15), p. 3188-3198
    Abstract: Serine proteinase inhibitors (serpins) are a family of structurally similar but functionally diverse proteins that regulate several important proteolytic cascades in most branches of life. We have characterized 17 Amblyomma americanum serpin cDNAs here named as `Lospins' (L; an acronym for Lone Star tick serpin) that possess three β-sheets, eight α-helices and a reactive center loop consistent with the consensus serpin superfamily secondary structures. Visual inspection of deduced amino acid sequences revealed two patterns of basic residues: (i) 86DKSRVLKAYKRL97 in L5 and L13–16 and (ii) 158VRDKTRGKI166 in all Lospins, which are similar to consensus glycosaminoglycan (GAG) binding sites (XBnXmBX, where X and B are non-basic and basic residues, n=1 or 2 and m=1, 2 or 3). On three-dimensional models, the two putative GAG binding sites mapped onto α-helices D and F, respectively, with calculation of electrostatic surface potentials revealing basic patches on L5 and L13–16 models that are comparable to the heparin-binding site on antithrombin. RT-PCR expression analysis of 15 selected genes showed that the majority (11/15) of the Lospins were ubiquitously expressed in the midgut, ovary and salivary glands. On a neighbor-joining phylogeny guide tree, 15 serpins from other ticks and 17 Lospins from this study, a total of 32 tick serpin sequences, segregated into five groups with Lospins in groups A and D being conserved across tick species. The discovery of Lospins in this study sets the framework for future studies to understand the role of serpins in tick physiology.
    Type of Medium: Online Resource
    ISSN: 1477-9145 , 0022-0949
    Language: English
    Publisher: The Company of Biologists
    Publication Date: 2007
    detail.hit.zdb_id: 1482461-9
    SSG: 12
    Location Call Number Limitation Availability
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  • 6
    Online Resource
    Online Resource
    Elsevier BV ; 2010
    In:  Insect Biochemistry and Molecular Biology Vol. 40, No. 7 ( 2010-07), p. 524-532
    In: Insect Biochemistry and Molecular Biology, Elsevier BV, Vol. 40, No. 7 ( 2010-07), p. 524-532
    Type of Medium: Online Resource
    ISSN: 0965-1748
    Language: English
    Publisher: Elsevier BV
    Publication Date: 2010
    detail.hit.zdb_id: 1483248-3
    SSG: 12
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