ORIGINAL_ARTICLE
Phenotypic and Molecular Screening of Tomato Germplasm for Resistance to Tomato Yellow Leaf Curl Virus
Tomato yellow leaf curl virus (TYLCV) is a major tomato virus in tropical and subtropical regions. In this study, 134 accessions of Solanum lycopersicum and six accessions of Solanum peruvianum were assessed for resistance to an Iranian isolate of TYLCV. Plants were inoculated using whiteflies (Bemisia tabaci) and the reaction of plants was evaluated based on either disease symptoms or viral DNA amplification. All accessions of S. lycopersicum had demonstrated various degrees of disease symptoms. However, all six accessions of S. peruvianum were resistant and remained symptomless. Phenotypic evaluation was confirmed by amplification of a 670bp TYLCV DNA fragment in all tested accessions of S. lycopersicum. Based on both phenotypic and molecular evaluations, no accession provided complete resistance to TYLCV, whereas nine accessions were assessed as tolerant. The high level of resistance noted in whitefly inoculated accessions of S. peruvianum was not observed in graft inoculated plants of these accessions. The TYLCV DNA fragment was detected five weeks post-inoculation when plants were inoculated by grafting. These results suggested that accessions of S. peruvianum may be merely resistant to vector inoculation of TYLCV.
https://www.ijbiotech.com/article_7037_dd9cda0e0df121a5d3204158dab23f4e.pdf
2008-10-01
199
206
Molecular screening
Tomato
TYLCV
Virus resistance
Abdulbaset
Azizi
1
National Plant Gene-Bank, Seed and Plant Improvement Institute, Mahdasht Road, P.O Box 31585-4119, Karaj, Iran
and
Department of Plant Pathology, Faculty of Agriculture,Tarbiat Modares University, P.O. Box 14115-326 Tehran, Iran
AUTHOR
Javad
Mozafari
jmozafar@yahoo.com
2
National Plant Gene-Bank, Seed and Plant Improvement Institute, Mahdasht Road, P.O Box 31585-4119, Karaj, Iran
LEAD_AUTHOR
Masoud
Shams-bakhsh
shamsbakhsh@gmail.com
3
Department of Plant Pathology, Faculty of Agriculture,Tarbiat Modares University, P.O. Box 14115-326 Tehran, Iran
AUTHOR
AVRDC (2001). AVRDC Report 2000, AVRDC, Taiwan. PP. 110-112.
1
Azizi A (2007). Screening of Iranian Tomato Germplasm for Resistance to Tomato yellow leaf curl virus (TYLCV), MSc thesis, Tarbiat Modares University, Tehran, Iran.
2
Chague V, Mercier JC, Guenard M, de Courcel A, Vedel F (1997). Identification of RAPDs markers linked to a locus involved in quantitative resistance to TYLCV in tomato by bulked segregant analysis. Theor Appl Genet. 95: 671-677.
3
Cohen S, Nitzany FE (1966). Transmission and host range of the tomato yellow leaf curl virus. Phytopathology 56: 1127-1131.
4
Delatte H, Holota H, Reynaud B, Dintinger J (2006). Characterisation of a quantitative resistance to vector transmission of Tomato yellow leaf curl virus in Lycopersicon pimpinellifolium. Europ J Plant Pathol. 114: 245-253.
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12
Lapidot M, Friedemann M, Pilowsky M, Ben-Joseph R, Cohen S (2001). Effect of host plant resistance to Tomato yellow leaf curl virus (TYLCV) on virus acquisition and transmission by its whitefly vector. Phytopathology 91: 1209-1213.
13
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14
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23
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24
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27
ORIGINAL_ARTICLE
Optimization of Transient Expression of uidA Gene in Androgenic Embryos of Wheat (Triticum aestivum L. cv. Falat) via Particle bombardment
Haploid microspore-derived embryos (MDEs) of wheat were obtained by in vitro androgenesis. These embryos were employed to evaluate the transient expression of GUS gene (uidA) following particle bombardment. Using the Bio-Rad PDS-1000/He system, the physical parameters including rupture disk pressure (900, 1100 and 1350 psi); microprojectile travel distance (6 and 9 cm); gold particles size (0.6 mm, 1 mm and 1.6 mm), DNA and microcarrier concentrations (0.5 mg of DNA with 150 μg of gold particles or 1.0 μg of DNA with 300 mg of gold particles/bombardment) and bombardment numbers (1x (single) and 2x (double)) were assessed. The effect of high osmoticum in the bombardment medium (0.3 M mannitol and 0.4 M maltose) and the age of embryos were also evaluated. Optimal expression in MDEs was obtained using the following conditions of double bombardment at 1350 psi, 9 cm target distance, a 1 mm gold particle size, 1.0 mg of DNA with 300 mg of gold particles/bombardment, and osmotic pretreatment of 4-6 weeks old embryos using 0.4 M maltose for 6 h before and 16 h after bombardment. The optimized transformation protocol presented in this study is expected to improve devalopment of commercial transgenic wheat lines expressing desirable agronomic traits.
https://www.ijbiotech.com/article_7038_5fc8dcea5e821c748d5ca561a33223ba.pdf
2008-10-01
207
213
Hexaploid wheat
Transient gene expression
GUS
Particle bombardment
Androgenic embryos
Shahrokh
Gharanjik
1
Department of Plant Breeding, Faculty of Agriculture, Tarbiat Modares University, P.O. Box 14115-336, Tehran, I.R. Iran
AUTHOR
Ahmad
Moieni
moieni_ahmad@yahoo.com
2
Department of Plant Breeding, Faculty of Agriculture, Tarbiat Modares University, P.O. Box 14115-336, Tehran, I.R. Iran
LEAD_AUTHOR
Amir
Mousavi
m-amir@nigeb.ac.ir
3
National Institute of Genetic Engineering and Biotechnology, P.O. Box 14965/161, Tehran, I.R. Iran
AUTHOR
Houshang
Alizadeh
halizade@ut.ac.ir
4
Department of Plant Breeding, Faculty of Agriculture, University of Tehran, P.O. Box 4111, Karaj, I.R. Iran
AUTHOR
Altpeter F, Baisakh N, Beachy R, Bock R, Capell T, Christou P, Daniell H, Datta K, Datta S, Dix PJ, Fauquet C, Huang N, Kohli A, Mooibroek H, Nicholson L, Nguyen TT, Nugent G, Raemakers K, Romano A, Somers DA, Stoger E, Taylor N, Visser R (2005). Particle bombardment and the genetic enhancement of crops: myths and realities. Mol Breed. 15: 305-327.
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39
ORIGINAL_ARTICLE
Isolation and Characterization of Thermophilic Alkaline Proteases Resistant to Sodium Dodecyl Sulfate and Ethylene Diamine Tetraacetic Acid from Bacillus sp. GUS1
Thermophilic Bacillus sp. GUS1, isolated from a soil sample obtained from citrus garden, produced at least three proteases as detected by sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE) and zymogram analysis. The enzymes were stable in the alkaline pH range (8.0-12.0), with the optimum temperature and pH range of the proteases being 70ºC and 6.0-12.0, respectively. All three proteases were also highly stable at 70ºC. After 60 min of incubation at 70ºC, the enzymes retained 100% of their original activities. Enzymes were mostly inhibited by phenylmethylsulfonyl fluoride (PMSF), however 80-90% enzyme activities were retained in presence of 2-mercaptoethanol and iodoacetate. Addition of SDS and ethylene diamine tetraacetic acid (EDTA) also marginally influenced protease activities, but addition of Ca2+ to the proteases did not bring about any change. The results suggeste that most of these proteases were not metalloproteases, but Ca2+-independent serine alkaline proteases.
https://www.ijbiotech.com/article_7039_6eb2271b1fe56ae87dd0756591916e81.pdf
2008-10-01
214
221
Bacillus sp
Alkaline serine proteases
Thermostability Resistance to EDTA and SDS
Sara
Seifzadeh
1
Department of Biology, Faculty of Science, University of Guilan, P.O. Box 41335-1914, Rasht, I.R. Iran
AUTHOR
Reza
Hassan Sajedi
2
Department of Biology, Faculty of Science, University of Guilan, P.O. Box 41335-1914, Rasht, I.R. Iran
LEAD_AUTHOR
Reyhaneh
Sariri
3
Department of Biology, Faculty of Science, University of Guilan, P.O. Box 41335-1914, Rasht, I.R. Iran
AUTHOR
Anwar A, Saleemuddin M (1998). Alkaline proteases: A review. Bioresour Technol. 64: 175-183.
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Beg QK, Saxena RK, Gupta R (2002). De-repression and subsequent induction of protease synthesis by Bacillus mojavensis under fed-batch operations. Process Biochem. 37: 1103-1109.
4
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43
ORIGINAL_ARTICLE
Evaluation of Nucleic Acid Sequence Based Amplification (NASBA) and Reverse Transcription Polymerase Chain Reaction for Detection of Coxsackievirus B3 in Cell Culture and Animal Tissue Samples
Enteroviruses are the causative agents of a number of diseases in humans. Group B coxsackieviruses are believed to be the most common viral agents responsible for human heart disease. Genomic data of enteroviruses has allowed developing new molecular approaches such as Nucleic Acid Sequence Based Amplification (NASBA) for detection of such viruses. In this study, coxsackievirus B3 (CVB3) was detected in virus-infected cell culture and specimens of artificially infected mice with specific primers using Reverse Transcription - Polymerase Chain Reaction (RT-PCR) and NASBA techniques. According to the results, both techniques could be used for the detection of viruses in cell culture and artificially infected animals. NASBA reaction was simpler to perform than RT-PCR. The only variable factor that had to be optimized with NASBA is KCl concentration. The optimal concentration of KCl was determined as 90 mM. Serial dilutions of 1 mg of total RNA showed that both RT-PCR and NASBA could detect the virus at 10-5 dilution. Analyses of heart and spleen samples from infected animals were positive for presence of Coxsackievirus B3 with both RT-PCR and NASBA. In conclusion, NASBA offers some advantages over RT-PCR and is a suitable alternative technique for the sensitive detection of CVB3 in contaminated samples.
https://www.ijbiotech.com/article_7041_c62751bfbf62526834d2a0a9c3de9db6.pdf
2008-10-01
222
228
Coxsackievirus B3
NASBA
RT-PCR
Alireza
Saeedinia
a_saeed54@hotmail.com
1
Department of Biotechnology, Maleke Ashtar University, P.O. Box 15875-1774, Tehran, I.R. Iran
LEAD_AUTHOR
Mehdi
Shamsara
2
Department of Animal Biotechnology, National Institute of Genetic Engineering and Biotechnology, P.O. Box 14965/161, Tehran, I.R. Iran
AUTHOR
Mehdi
Zeinoddini
3
Department of Biotechnology, Maleke Ashtar University, P.O. Box 15875-1774, Tehran, I.R. Iran
AUTHOR
Vahid
Sadeghi
4
Department of Biotechnology, Maleke Ashtar University, P.O. Box 15875-1774, Tehran, I.R. Iran
AUTHOR
Nader
Maghsoudi
5
Neuroscience Research Center, Shahid Beheshti Medical University, P.O. Box 16765-3718, Tehran, I.R. Iran
AUTHOR
Baboonian C, Davies MJ, Booth JC, Mc Kenna WJ (1997). Coxsackie B viruses and human heart disease. In: The coxsackie B viruses. Berlin-Heidelberg, Springer Verlag. pp. 31-52.
1
Bowles NE, Archard LC, Olsen EGJ, Richardson PJ (1986). Detection of Coxsackie-B-virus-specific RNA sequences in myocardial biopsy samples from patients with myocarditis and dilated cardiomyopathy. Lancet 1: 1120-1123.
2
Bowles NE, Towbin JA (2000). Molecular aspects of myocarditis. Curr Infec Dise Repo. 2: 308-314.
3
Capaul SE, Gorgievski-Hrisoho M (2005). Detection of enterovirus RNA in cerebrospinal fluid (CSF) using NucliSens EasyQ Enterovirus assay. J Clin Virol. 32: 236-240.
4
Chan AB, Fox JD (1999). NASBA and other transcription-based amplification methods for research and diagnostic microbiology. Rev Med Microbiol. 10: 185-196.
5
Compton J (1991). Nucleic acid sequence-based amplification. Nature 350: 91-92.
6
Cook N (2003). The use of NASBA for detection of microbial pathogens in food and environmental samples. J Microbiol Meth. 52: 165-174.
7
Deiman B, van Aarle P, Sillekens P (2002). Characteristics and applications of nucleic acid sequence-baced amplification (NASBA). Mol Biotechnol. 20: 163-179.
8
Fox JD, Han S, Samuelson A, Zhang Y, Neale ML, Westmoreland D (2002). Development and evaluation of nucleic acid sequence based amplification (NASBA) for diagnosis of enterovirus infections using the nucli-sens® Basic kit. J Clin Virol. 24: 117-130.
9
Fykse EM, Skogan G, Davies W, Olsen JS, Blatny JM (2007). Detection of Vibrio cholerae by real-time nucleic acid sequence-based amplification. Appl Environ Microbiol. 73: 1457-1466.
10
Ginocchio CC, Zhang F, Malhotra A, Manji R, Sillekens P, Foolen H, Overdyk M, Peeters M (2005). Development, technical performance, and clinical evaluation of a NucliSens basic kit application for detection of enterovirus RNA in cerebrospinal fluid. J Clin Microbiol. 43: 2616-2623.
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Grasso M, Arbustini E, Silini E, Diegoli M, Percivalle E, Ratti G, Bramerio M, Gavazzi A, Vigano M, Milanesi G (1992). Search for Coxsackievirus B3 RNA in idiopathic dilated cardiomyopathy using gene amplification by polymerase chain reaction. Am J Cardiol. 69: 658-664.
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Heim A, Schumann J (2002). Development and evaluation of a nucleic acid sequence-based amplification (NASBA) protocol for the detection of enterovirus RNA in corebrospiral fluid samples. J Virol Meth. 103: 101-107.
13
Houde A, Leblanc D, Poitras E, Ward P, Brassard J, Simard C, Trottier YL (2006). Comparative evaluation of RT-PCR, nucleic acid sequence-based amplification (NASBA) and real-time RT-PCR for detection of noroviruses in faecal material. J Virol Methods. 135: 163-172.
14
Jean J, Blais B, Darveau A, Fliss I (2001). Detection of hepatitis A virus by the nucleic acid sequence- based amplification technique and comparison with reverse transcription-PCR. Appl Envir Microbiol. 67: 5593-5600.
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Jean J, D’Souza DH, Jaykus LA (2004). Multiplex nucleic acid sequence-based amplification for simultaneous detection of several enteric viruses in model ready-to-eat foods. Appl Environ Microbiol. 70: 6603-6610.
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Leone G, Van Schijndel H, Van Gemen B, Kramer FR, Schoen CD (1998). Molecular beacon probes combined with amplification by NASBA enable homogeneous, real time detection of RNA. Nuc A Res. 26: 2150-2155.
22
Loens K, Beck T, Goossens H, Ursi D, Overdijk M, Sillekens P, Ieven M (2006). Development of conventional and real-time nucleic acid sequence-based amplification assays for detection of Chlamydophila pneumoniae in respiratory specimens. J Clin Microbiol. 44: 1241-1244.
23
Loens K, Goossens H, de Laat C, Foolen H, Oudshoorn P, Pattyn S, Sillekens P, Ieven M (2006). Detection of rhinoviruses by tissue culture and two independent amplification techniques, nucleic acid sequence-based amplification and reverse transcription-PCR, in children with acute respiratory infections during a winter season. J Clin Microbiol. 44: 166-171.
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27
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30
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31
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36
ORIGINAL_ARTICLE
Site-Directed Mutagenesis in Human Granulocyte-colony Stimulating Factor, Cloning and Expression in Escherichia coli
Human granulocyte colony stimulating factor (hG-CSF) induces proliferation and differentiation of granulocyte progenitor cells. This glycoprotein is currently being used for treatment of neutropenia, in patients who have undergone bone marrow transplantation. So far, different researchers have tried to enhance hG-CSF biological activity and stability. In this study, Polymerase Chain Reaction (PCR) based site-directed mutagenesis was performed on hG-CSF cDNA. The final amplified DNA fragment was cloned into the pBluescript sk(-) plasmid and after verification of the desired mutations by sequencing, it was subcloned into the pET-21a(+) vector and expressed in Escherichia coli BL21. The mutant G-CSF product was analyzed by SDS-PAGE and Western-blot analyses. The results show that the recombinant mutant G-CSF has been cloned and expressed successfully in prokaryotic system. This research aimed to produce a new recombinant hG-CSF expected to show enhanced biological characteristics in contrast to those of the native hG-CSF. The analysis of its function and biological characteristics remain to be examined.
https://www.ijbiotech.com/article_7044_6cfb61ad20766f62e1d4f80a35f1b5a6.pdf
2008-10-01
229
234
Granulocyte colony stimulating factor (G-CSF)
Site-directed mutagenesis
Expression
Hamed
Naghoosi
1
Department of Microbiology, Faculty of Science, Islamic Azad University, Karaj Branch, P.O. Box 31485-313, Karaj, I.R. Iran
AUTHOR
Farida
Behzadian
fbehzadian@yahoo.com
2
Department of Genetic Engineering, Research Center for Science and Biotechnology, P.O. Box 19395-1949, Tehran, I.R. Iran
LEAD_AUTHOR
Alireza
Saeedinia
3
Department of Genetic Engineering, Research Center for Science and Biotechnology, P.O. Box 19395-1949, Tehran, I.R. Iran
AUTHOR
Seyed Ali
Ghorashi
4
Department of Animal Biotechnology, National Institute of Genetic Engineering and Biotechnology, P.O. Box 14965/161, Tehran, I.R. Iran
AUTHOR
Bishop B, Koay DC, Sartorelli AC, Regan L (2001). Reengineering granulocyte colony-stimulating factor for enhanced stability. J Biol Chem. 276: 33465-33470.
1
Creighton Thomas E (1999). Encyclopedia of Molecular Biology, John Wily & Sons Inc. New York, USA.
2
Devlin Patricia E, Drummond Robert J, Toy Pam, Mark David F, Watt Kenneth WK, Devlin James J (1988). Alteration of amino-terminal codons of human granulocyte-colony-stimulating factor increases expression levels and allows efficient processing by methionine aminopeptidase in Escherichia coli. Gene 65: 13-22.
3
Fernández-Varón E, Villamayor L (2007). Granulocyte and granulocyte macrophage colony-stimulating factors as therapy in human and veterinary medicine. Vet J. 174: 33-41.
4
Hill Christopher P, Osslund Timothy D, Eisenberg D (1993). The structure of granulocyte-colony-stimulating factor and its relationship to other growth factors. Proc Natl Acad Sci USA. 90: 5167-5171.
5
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6
Ishikawa M, Okada Y, Ishikawa R, Tsumura H, Matsuki S, Asano K (1993). Protein tailoring of human granulocyte colony-stimulating factor. Biotechnol Lett. 15: 673-678.
7
Klingemann Hans-G (1989). Clinical applications of recombinant human colony-stimulating factors. CMAJ. 140: 137-142.
8
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9
Lu HS, Clogston CL, Narhi LO, Merewether LA, Pearl WR, Boone TC (1992). Folding and oxidation of recombinant human granulocyte colony stimulating factor produced in Escherichia coli, J Biol Chem. 267: 8770-8777.
10
Lu HS, Fausset PR, Narhi LO, Horan T, Shinagawa K, Shimamoto G, Boone TC (1999). Chemical modification and site-directed mutagenesis of methionine residues in recombinant human granulocyte colony-stimulating factor: Effect on stability and biological activity. Arch Biochem Biophys. 362: 1-11.
11
Luo Peizhi, Heyes Robert J, Chan Cheryl, Stark Dian M, Hwang Marian Y, Jacinto Jonathan M, Juvvadi Padmaja, Chung Helen S, Kundu A, Ary ML, Dahiyat BI (2002). Development of a cytokine analog with enhanced stability using computational ultrahigh throughput screening, Protein Sci. 11: 1218-1226.
12
Nagata S, Tsuchiya M, Asano S, Kaziro Y, Yamazaki T, Yamamoto O, Hirata Y, Kubota N, Oheda M, Nomura H, Ono M (1986a). Molecular cloning and expression of cDNA for human granulocyte colony-stimulating factor. Nature 319: 415-418.
13
Nagata S (1989). Gene structure and function of granulocyte colony-stimulating factor. Bio Essays 10: 113-117.
14
Nagata S, Tsuchiya M, Asano S, Yamamoto O, Hirata Y, Kubata N, Oheda M, Nomura H, Yamazaki T (1986b). The chromosomal gene structure and two mRNAs for human granulocyte colony-stimulating factor. EMBO J. 5: 575-581.
15
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16
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17
Oshima Yasuo, Tojo Arinobu, Niho Yoshiyuki, Asano Shigetaka, (2000), Biological Activity of Human Granulocyte Colony Stimulating Factor with a Modified C-Terminus. Biochem Biophys Res Commun. 267: 924-927.
18
Reidhaar-Olson John F, De Souza-Hart Janet A, Selick Harold E (1996). Identification of residues critical to the activity of human granulocyte colony-stimulating factor. Biochemistry 35: 9034-9041.
19
Saeedinia A, Sadeghizadeh M, Maghsoudi N, Fallah Mehrabadi J, Karimi M, Akbari B (2003). Construction and cloning of human granulocyte colony stimulating factor (hG-CSF) cDNA. Modarres JMS (in Persian). 5: 1.
20
Sambrook J, Russel DW (2001). Molecular Cloning: a laboratory manual, Cold Spring Harbor Laboratory Press. New York, USA.
21
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22
Yamasaki M, Konishi N, Yamaguchi K, Itoh S, Yokoo Y (1998). Purification and characterization of recombinant human granulocyte colony-stimulating factor (rhG-CSF) derivatives: KW-2228 and other derivatives. Biosci Biotechnol Biochem. 62: 1528-1534.
23
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24
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25
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26
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27
ORIGINAL_ARTICLE
Sequence Analysis of M2 Gene of Avian Influenza Virus Strain (A/Chicken/Iran/101/98 (H9N2)) as an Oil Vaccine Seed
In this study, the full-length M2 gene of the avian influenza virus (H9N2) was isolated, analyzed and studied in detail. Total RNA was extracted and cDNA of the M2 mRNA was obtained by reverse transcriptase polymerase chain reaction (RT-PCR) using random hexamer oligoes; specific primers were used for amplification of the M2 open reading frame (ORF) region. PCR was able to amplify the desirable fragment (294-bp) of the spliced M2 gene. The nucleotide sequence homology between the Iranian isolate and other H9 and H5 subtypes of influenza A from different hosts and geographical areas deposited in GenBank ranged from 92 to 98% and the amino acid sequence homology ranged from 97 to 100%.
https://www.ijbiotech.com/article_7045_e85288408b415eba6c71267614304a5f.pdf
2008-10-01
235
138
M2 gene
Sequence
RT-PCR
H9N2
Seyed Mahmoud
Ebrahimi
smebrahimi@shirazu.ac.ir; s.ebrahimi@rvsri.ir
1
Department of Biotechnology, Razi vaccine and serum research Institute, P.O. Box 31975/148, Karaj, Ira
and
Department of Avian Medicine, School of Veterinary Medicine, Shiraz University, P.O. Box 1731, Shiraz, Iran
LEAD_AUTHOR
Khosrow
Aghaiypour
2
Department of Biotechnology, Razi vaccine and serum research Institute, P.O. Box 31975/148, Karaj, Iran
AUTHOR
Hassan
Nili
3
Department of Avian Medicine, School of Veterinary Medicine, Shiraz University, P.O. Box 1731, Shiraz, Iran
AUTHOR
Bauer CM, Pinto LH, Cross TA, Lamb RA (1999).The influenza virus M2 ion channel protein: probing the structure of the transmembrane domain in intact cells by using engineered disulfide cross-linking. Virology 254: 196-209.
1
Hay AJ, Wolstenholme AJ, Skehel JJ, Smith MH (1985). The molecular basis of the specific anti-influena action of amantadine. EMBO J. 4: 3021-3024.
2
Holsinger LJ, Lamb RA (1991). Influenza virus M2 integral membrane protein is a homotetramer stabilized by formation of disulfide bonds. Virology 183: 32-43.
3
Lamb RA, Zebedee SL, Richardson CD (1985). Influenza virus M2 protein is an integral membrane protein expressed on the infected-cell surface. Cell 40: 627-633.
4
Neirynck S, Deroo T, Saelens X, Vanlandschoot P, Jou WM, Fiers W (1999). A universal influenza A vaccine based on the extracellular domain of the M2 protein. Nat Med. 5: 1157-1163.
5
Pinto LH, Holsinger IJ, Lamb RA. (1992). Influenza virus M2 protein has ion channel activity. Cell 69: 517-528.
6
Webster RG, Bean WJ, Gorman OT, Chambers TM, Kawaoka Y (1992). Evolution and ecology of influenza A viruses. Microbiol Rev. 56: 152-179.
7
Widjaja L, Krauss SL, Webby RJ, Xie T, Webster RG (2004). Matrix gene of influenza A viruses isolated from wild aquatic birds: Ecology and emergence of influenza A virus. Virology 78: 8771-8779.
8
Zebedee SL, Lamb RA (1988). Influenza A virus M2 protein: monoclonal antibody restriction of virus growth and detection of M2 in virions. Virology 62: 2762-2767.
9