کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
2830288 | 1163374 | 2007 | 7 صفحه PDF | دانلود رایگان |
عنوان انگلیسی مقاله ISI
Molecular cloning and characterization of a C-type lectin from Ancylostoma ceylanicum: Evidence for a role in hookworm reproductive physiology
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کلمات کلیدی
NCBIIPTGHRPRT-PCRAncylostoma ceylanicum3′RACEsodium dodecyl sulphate-polyacrylamide gel electrophoresis - الکتروفورز ژل دوده سولفات سدیم پلی آکریل آمیدSDS-PAGE - الکتروفورز ژل پلی آکریل آمیدSperm - اِسپِرمisopropyl-β-d-thiogalactopyranoside - ایزوپروپیل-ب-دی-تیوگالکتوپیرانوزیدC-type lectin - لکتین نوع CNational Center for Biotechnology Information - مرکز ملی اطلاعات بیوتکنولوژیreverse transcription polymerase chain reaction - واکنش زنجیره ای پلیمراز رونویسی معکوسHorseradish peroxidase - پراکسیداز هوررادیشHookworm - کرم هوکNematode - کرمهای لولهای
موضوعات مرتبط
علوم زیستی و بیوفناوری
بیوشیمی، ژنتیک و زیست شناسی مولکولی
زیست شناسی مولکولی
پیش نمایش صفحه اول مقاله
![عکس صفحه اول مقاله: Molecular cloning and characterization of a C-type lectin from Ancylostoma ceylanicum: Evidence for a role in hookworm reproductive physiology Molecular cloning and characterization of a C-type lectin from Ancylostoma ceylanicum: Evidence for a role in hookworm reproductive physiology](/preview/png/2830288.png)
چکیده انگلیسی
Lectins comprise a family of related proteins that mediate essential cell functions through binding to carbohydrates. Within this protein family, C-type lectins are defined by the requirement of calcium for optimal biologic activity. Using reverse transcription PCR, a cDNA corresponding to a putative C-type lectin has been amplified from the hookworm parasite Ancylostoma ceylanicum. The 550 nucleotide open reading frame of the A. ceylanicum C-type Lectin-1 (AceCTL-1) cDNA corresponds to a 167 amino acid mature protein (18,706Â Da) preceded by a 17 amino acid secretory signal sequence. The recombinant protein (rAceCTL-1) was expressed in Drosophila S2 cells and purified using a combination of affinity chromatography and reverse phase HPLC. Using in vitro carbohydrate binding studies, it was determined that rAceCTL-1 binds N-acetyl-d-glucosamine, a common component of eukaryotic egg cell membranes. Using a polyclonal IgG raised against the recombinant protein, the native AceCTL-1 was identified in sperm and soluble protein extracts of adult male A. ceylanicum by immunoblot. Probing of adult hookworm sections with the polyclonal IgG demonstrated localization to the testes in males, as well as the spermatheca and developing embryos in females, consistent with its role as a sperm protein. Together, these data strongly suggest that AceCTL-1 is a male gender-specific C-type lectin with a function in hookworm reproductive physiology.
ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Molecular and Biochemical Parasitology - Volume 151, Issue 2, February 2007, Pages 141-147
Journal: Molecular and Biochemical Parasitology - Volume 151, Issue 2, February 2007, Pages 141-147
نویسندگان
Allison C. Brown, Lisa M. Harrison, Wadim Kapulkin, Brian F. Jones, Anindita Sinha, Amy Savage, Nicholas Villalon, Michael Cappello,