Solenopsis invicta transferrin:: cDNA cloning, gene architecture, and up-regulation in response to Beauveria bassiana infection

被引:32
作者
Valles, SM [1 ]
Pereira, RM [1 ]
机构
[1] ARS, Ctr Med Agr & Vet Entomol, USDA, Gainesville, FL 32608 USA
关键词
transferrin; Solenopsis invicta; Q-PCR; gene expression;
D O I
10.1016/j.gene.2005.05.017
中图分类号
Q3 [遗传学];
学科分类号
071007 ; 090102 ;
摘要
Transferrin genes from several insects have been shown to be induced in response to bacterial or fungal infection. We were interested to know whether transferrin genes in the red imported fire ant, Solenopsis invicta, are similarly induced by microbial challenge. Hence, the cDNA and structure of a gene exhibiting significant homology to insect transferrins were elucidated for S. invicta. The cDNA was comprised of 2417 nucleotides, excluding the poly(A) tail, with a large open reading frame of 2106 nucleotides. The predicted translation product of the S. invicta tranferrin (SiTf) gene was a 702 amino acid polypeptide with an estimated molecular mass of 77.3 kDa and a pI value of 5.66, characteristics consistent with transferrin proteins. Comparative analysis of genomic and cDNA sequences revealed that the SiTf gene was comprised of 8 exons. Quantitative real-time PCR was used to examine the expression of SiTf. Expression of SiTf was induced in worker ants exposed to Beauveria bassiana conidia. Autoclave-killed conidia did not elicit a SiTf induction response from worker ants. Genes, like SiTf, responding to microbe attack or infection may provide a unique approach to assist in the discovery of microbial control organisms for the target insect pest. Published by Elsevier B.V.
引用
收藏
页码:60 / 66
页数:7
相关论文
共 35 条
[1]   THE REGION OF HUMAN TRANSFERRIN INVOLVED IN BINDING TO BACTERIAL TRANSFERRIN RECEPTORS IS LOCALIZED IN THE C-LOBE [J].
ALCANTARA, J ;
YU, RH ;
SCHRYVERS, AB .
MOLECULAR MICROBIOLOGY, 1993, 8 (06) :1135-1143
[2]   Cloning and expression of a putative transferrin cDNA of the spruce budworm, Choristoneura fumiferana [J].
Ampasala, DR ;
Zheng, SC ;
Retnakaran, A ;
Krell, PJ ;
Arif, BM ;
Feng, QL .
INSECT BIOCHEMISTRY AND MOLECULAR BIOLOGY, 2004, 34 (05) :493-500
[3]   STRUCTURE OF HUMAN LACTOFERRIN - CRYSTALLOGRAPHIC STRUCTURE-ANALYSIS AND REFINEMENT AT 2.8-A RESOLUTION [J].
ANDERSON, BF ;
BAKER, HM ;
NORRIS, GE ;
RICE, DW ;
BAKER, EN .
JOURNAL OF MOLECULAR BIOLOGY, 1989, 209 (04) :711-734
[4]   Lactoferrin and transferrin: Functional variations on a common structural framework [J].
Baker, EN ;
Baker, HM ;
Kidd, RD .
BIOCHEMISTRY AND CELL BIOLOGY-BIOCHIMIE ET BIOLOGIE CELLULAIRE, 2002, 80 (01) :27-34
[5]  
BARTFELD NS, 1990, J BIOL CHEM, V265, P21684
[6]  
BREATHNACH R, 1981, ANNU REV BIOCHEM, V50, P349, DOI 10.1146/annurev.bi.50.070181.002025
[7]   Binding and surface exposure characteristics of the gonococcal transferrin receptor are dependent on both transferrin-binding proteins [J].
Cornelissen, CN ;
Sparling, PF .
JOURNAL OF BACTERIOLOGY, 1996, 178 (05) :1437-1444
[8]  
Dimarcq JL, 1998, BIOPOLYMERS, V47, P465, DOI 10.1002/(SICI)1097-0282(1998)47:6<465::AID-BIP5>3.0.CO
[9]  
2-#
[10]   Cockroach transferrin closely resembles vertebrate transferrins in its metal ion-binding properties: A spectroscopic study [J].
Gasdaska, JR ;
Law, JH ;
Bender, CJ ;
Aisen, P .
JOURNAL OF INORGANIC BIOCHEMISTRY, 1996, 64 (04) :247-258