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Bangalore H. Durgesh, Abdulaziz A. Alkheraif, Asmaa M. Malash, Mohamed I. Hashem, Mansour K. Assery, Mohammed Al Asmari and Pavithra Durgesh

by performing specific gene uniplex polymerase chain reaction (PCR) for E. faecalis and E. faecium as previously described [ 3 ]. Identification of putative virulence genes; efaA (gene for endocarditis), gelE (gene for gelatinase), ace (gene for collagen binding antigen), asa (gene for aggregation substance), cylA (gene for cytolysin activator), and esp (gene for surface adhesin) of E. faecalis and E. faecium were performed as described previously ( Table 1 ) . Table 1 Primers used to identify species and to detect the virulence genes

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Supathra Tiewcharoen, Jundee Rabablert, Sittiruk Roytrakul, Waravee Wiyawuth, Nat Malainual, Virach Junnu, Kumchol Chaiyo and Prasert Auewarakul

, Lin J, et al. Comparing gene discovery from Affymetrix GeneChip microarrays and Clontech PCR-select cDNA subtraction: a case study. BMC Genomics. 2004; 5: 26. 10. Lacrue AN, Jamus AA, Beerntsen BT. The novel Plasmodium gallinaceum sporozoite protein, Pg93, is preferentially expressed in the nucleus of oocyst sporozoites. Am J Trop Med Hyg. 2005; 73:634-43. 11. Florent I, Porcel BM, Guillaume E, Silva CD, Artiguenave F, Maréchal E, et al. A Plasmodium falciparum FcB1-schizont-EST collection providing clues to schizont specific gene

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Suda Louisirirotchanakul, Pornparn Rojanasang, Kleophant Thakerngpol, Naree Choosrichom, Kridsda Chaichoune, Phisanu Pooruk, Aphinya Namsai, Robert Webster and Pilaipan Puthavathana

Abstract

Background: An outbreak of highly pathogenic avian influenza (HPAI) H5N1 virus in Thailand was first reported in 2004. To date, electron micrographs demonstrating the morphology of HPAI H5N1 virus particle are quite limited.

Objective: To demonstrate the morphology of HPAI H5N1 virus particles, avian influenza viruses with low pathogenicity, seasonal influenza viruses, and H5N1 structural components in infected cells. The M amino acid residues that might affect the viral morphology were also analyzed.

Methods: Electron micrographs of negatively-stained virus particles and positively-stained thin sections of the HPAI H5N1 virus infected cells were visualized under a transmission electron microscope. M amino acid sequences of the study viruses were retrieved from the GenBank database and aligned with those of reference strains with known morphology and residues that are unique for the morphological type of the virus particles.

Results: Morphologically, three forms of influenza virus particles, spherical, regular, and irregular rods, and long filamentous particles, were demonstrated. However, the spherical form was the most predominant morphological type and accounted for more than 80% of the virus populations examined. In addition, the viral entry and exit steps including incomplete particles in infected Madin-Darby canine kidney cells were visualized. Our analyses did not find any M amino acid residues that might influence the viral morphology.

Conclusion: Of all virus isolates studied, we demonstrated that the spherical particles were the major population observed regardless of virus subtype, host of origin, virus virulence, or passage history. Our study suggested that the morphology of influenza virus particles released, might not be strongly influenced by M gene polymorphism.

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Mongkol Pongsuchart, Amornpun Sereemaspun and Kiat Ruxrungtham

detection of infectious spleen and kidney necrosis virus by loop-mediated isothermal amplification combined with a lateral flow dipstick. Archives of Virology. 2010; 155:385-9. 7. Odenthal KJ, Gooding JJ. An introduction to electrochemical DNAbiosensors. Analyst. 2007; 132: 603-10. 8. Noguera P, Posthuma-Trumpie G, van Tuil M, van der Wal F, de Boer A, Moers A, et al. Carbon nanoparticles in lateral flow methods to detect genes encoding virulence factors of Shiga toxin-producing Escherichia coli. Analytical and Bioanalytical Chemistry. 2011

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Andika C. Putra, Keiji Tanimoto, Elisna Syahruddin, Sita Andarini, Yoshio Hosoi and Keiko Hiyama

. Novel CFTR mutations in a Korean infant with cystic fibrosis and pancreatic insufficiency. J Korean Med Sci. 2010; 25:163-5. 6. Collins F. Genetics terminology for respiratory physicians. Paediatr Respir Rev. 2009; 10:124-33. 7. Fu J, Festen EA, Wijmenga C. Multi-ethnic studies in complex traits. Hum Mol Genet. 2011; 20:R206-13. 8. Ober C, Hoffjan S. Asthma genetics 2006: the long and winding road to gene discovery. Genes Immun. 2006; 7:95-100. 9. Moffatt MF, Kabesch M, Liang L, Dixon AL, Strachan D

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Warisa Amornrit, Veerachat Muangsombut, Tanapol Wangteeraprasert and Sunee Korbsrisate

expression in Caco-2 human intestinal cells. J Nutr. 2001; 131:1452-8. 8. Bullen JJ, Ward CG, Wallis SN. Virulence and the role of iron in Pseudomonas aeruginosa infection. Infect Immun. 1974; 10:443-50. 9. Wuthiekanun V, Smith MD, Dance DA, White NJ. Isolation of Pseudomonas pseudomallei from soil in north-eastern Thailand. Trans R Soc Trop Med Hyg. 1995; 89:41-3. 10. Schaible UE, Kaufmann SH. Iron and microbial infection. Nat Rev Microbiol. 2004; 2:946-53. 11. Loprasert S, Sallabhan R, Whangsuk W, Mongkolsuk

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Wichit Thaveekarn, Sunchai Payungporn, Narumol Pakmanee, Sunutcha Suntrarachun, Suchitra Khunsap and Suthidee Petsong

PE-PGRS family protein. PE-PGRS is a large family of typical proteins of pathogenic mycobacteria whose members are characterized by an N-terminal PE domain followed by a large Gly-Ala repeat-rich C-terminal domain [ 18 ]. The genes of the PE-PGRS family proteins are most often clustered in a region of the genome, often as overlapping genes. The proline- glutamic acid (PE) domain is responsible for the cellular localization of these proteins on bacterial cells [ 19 ]. The hypothetical proteins found 3 positions shown in Table 1 might be involved in virulence

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Panan Kanchanaphum and Jerapan Krungkrai

pathology in malaria infections? Immunol Today. 1999; 20:228-33. 5. Dondorp AM, Nosten F, Yi P, Das D, Phyo AP, Tarning J, et al. Artemisinin resistance in Plasmodium falciparum malaria. N Engl J Med. 2009; 361:455-67. 6. Htut ZW. Artemisinin resistance in Plasmodium falciparum malaria. N Engl J Med. 2009; 361:1807-8. 7. Stein WD, Sanchez CP, Lanzer M. Virulence and drug resistance in malaria parasites. Trends Parasitol. 2009; 25:441-3. 8. Krungkrai J, Krungkrai S. Malaria parasite: Genomics, biochemistry and

Open access

Pawana Panomket

-701. 23. Vorachit M, Lam K, Jayanetra P, Costerton JW. Electron microscopy study of the mode of growth of Pseudomonas pseudomallei in vitro and in vivo. J Trop Med Hyg. 1995; 98:379-91. 24. Taweechaisupapong S, Kaewpa C, Arunyanart C, Kanla P, Homchumpa P. Virulence of Burkholderia pseudomallei does not correlate with biofilm formation. Microb Pathog. 2005; 39:77-85. 25. Vorachit M, Lam K, Jayanetra P, Costerton JW. Resistance of Pseudomonas pseudomallei growing as a biofilm on silastic disc to ceftazidime and cotrimoxazole. Antimicrob

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Gulcan Sahal and Isil Seyis Bilkay

crystals [ 5 , 6 ]. These crystals are deposited directly onto the catheter surface or into microbial biofilms; leading to blockage and encrustation of catheters, retention of urine in the bladder and development of bacteriuria [ 2 , 6 ]. Previous reports showed a correlation between biofilm production and multiple drug resistance in clinical isolates [ 7 - 8 ]. Increased antibiotic resistance is thought to be related to biofilm formation. This increased resistance is related to gene transfer within biofilms [ 9 ]. The aim of this study was to determine the clinical