scholarly journals Genetic Loci of Major Antigenic Protein Genes of Edwardsiella tarda

2005 ◽  
Vol 71 (9) ◽  
pp. 5654-5658 ◽  
Author(s):  
Noel Verjan ◽  
Ikuo Hirono ◽  
Takashi Aoki
Keyword(s):  
Polyclonal Antiserum ◽  
Japanese Flounder ◽  
Amino Acid Sequences ◽  
Edwardsiella Tarda ◽  
Membrane Stress ◽  
Subunit Vaccines ◽  
Antigenic Protein ◽  
Rabbit Polyclonal Antiserum ◽  
Antigenic Proteins ◽  
Periplasmic Proteins

ABSTRACT Seven antigenic proteins of Edwardsiella tarda were identified by using a rabbit polyclonal antiserum. Four of these proteins also reacted with a Japanese flounder antiserum. The amino acid sequences had identity to lipoproteins, periplasmic proteins, and exported and secreted proteins with roles in transport of metabolites across the cell membrane, stress response, and motility. These genes and their products are useful for developing DNA or recombinant subunit vaccines to control edwardsiellosis.

scholarly journals Identification of Major Antigenic Proteins of Edwardsiella Tarda Recognized by Japanese Flounder Antibody

2009 ◽  
Vol 21 (4) ◽  
pp. 504-509 ◽  
Author(s):  
Takamitsu Sakai ◽  
Tomomasa Matsuyama ◽  
Toyohiro Nishioka ◽  
Chihaya Nakayasu ◽  
Takashi Kamaishi ◽  
...  
Keyword(s):  
Japanese Flounder ◽  
Edwardsiella Tarda ◽  
Antigenic Proteins

scholarly journals Sensitive and Rapid Detection of Edwardsiellosis in Fish by a Loop-Mediated Isothermal Amplification Method

2004 ◽  
Vol 70 (1) ◽  
pp. 621-624 ◽  
Author(s):  
Ram Savan ◽  
Arisa Igarashi ◽  
Satoru Matsuoka ◽  
Masahiro Sakai
Keyword(s):  
Rapid Detection ◽  
Japanese Flounder ◽  
Isothermal Amplification ◽  
Edwardsiella Tarda ◽  
Fish Disease ◽  
Fish Pathogen ◽  
Loop Mediated Isothermal Amplification ◽  
Diagnostic Protocol ◽  
Amplification Method ◽  
Hemolysin Gene

ABSTRACT Here we report a rapid and sensitive method (using loop-mediated isothermal amplification [LAMP]) for the diagnosis of edwardsiellosis, a fish disease caused by Edwardsiella tarda, in Japanese flounder. A set of four primers was designed, and conditions for the detection were optimized for the detection of E. tarda in 45 min at 65°C. No amplification of the target hemolysin gene was detected in other related bacteria. When the LAMP primers were used, detection of edwardsiellosis in infected Japanese flounder kidney, and spleen and seawater cultures was possible. We have developed a rapid and sensitive diagnostic protocol for edwardsiellosis detection in fish. This is the first report of the application of LAMP for the diagnosis of a fish pathogen.

scholarly journals A Serological Study on Edwardsiella tarda Strains Isolated from Diseased Japanese Flounder(Paralichthys olivaceus).

1994 ◽  
Vol 29 (4) ◽  
pp. 277 ◽  
Author(s):  
M. Mamnur Rashie ◽  
Takayuki Mekuchi ◽  
Toshihiro Nakai ◽  
Kiyokuni Muroga
Keyword(s):  
Paralichthys Olivaceus ◽  
Japanese Flounder ◽  
Edwardsiella Tarda ◽  
Serological Study

PROTEASE NEXIN II IN HUMAN PLATELETS.

1987 ◽  
Author(s):  
W E Van Nostrand ◽  
P P Cunningham
Keyword(s):  
Growth Factor ◽  
Human Fibroblasts ◽  
Human Platelets ◽  
Polyclonal Antiserum ◽  
Single Chain ◽  
Gamma Subunit ◽  
Apparent Homogeneity ◽  
Rabbit Polyclonal Antiserum ◽  
Cultured Human Fibroblasts ◽  
Protease Nexin

Normal human fibroblasts secrete a protein into the culture medium named protease nexin II (PN II), which forms sodium do-decyl sulfate (SDS)-stable complexes with epidermal growth factor binding protein (EGF BP). These complexes then bind back to the same cells and are rapidly internalized and degraded. We recently purified PN II to apparent homogeneity and showed that it is a single chain polypeptide with an estimated molecular weight of 106 KDa. Other interesting properties of this protein include its ability to bind heparin and its stability to treatment with SDS or pH 1.5. In addition to EGF BP, PN II will also complex the gamma subunit of 7S nerve growth factor (NGF-gamma) and trypsin. Here we show that human platelets contain a protein which possesses the same properties as does PN II from cultured human fibroblasts. This platelet PN II (PL-PN II) is also a 106 KDa single chain polypeptide which can complex EGF BP, NGF-gamma and trypsin. PL-PN II also possesses the unusual stability to treatment with SDS or pH 1.5. In addition, both PN II and PL-PN II exhibit the same affinity for binding to heparin-Sepharose. Furthermore, rabbit polyclonal antiserum raised against PN II recognized PL-PN II on Western blot analysis demonstrating that both proteins are immunologically related. Treatment of fresh unactivated platelets with epinephrine or thrombin resulted in a release of PL-PN II into the supernatant suggesting that PL-PN II is stored in the platelet alpha granules.

scholarly journals Toxigenic clostridia.

1990 ◽  
Vol 3 (1) ◽  
pp. 66-98 ◽  
Author(s):  
C L Hatheway
Keyword(s):  
Amino Acid ◽  
Biological Activities ◽  
Amino Acid Sequences ◽  
Biologically Active ◽  
Antigenic Protein ◽  
Historical Aspects ◽  
Biochemical Characteristics ◽  
Animal Diseases ◽  
Human And Animal Diseases ◽  
Binary Toxins

Toxigenic clostridia belonging to 13 recognized species are discussed in this review. Each species or group of organisms is, in general, introduced by presenting the historical aspects of its discovery by early investigators of human and animal diseases. The diseases caused by each species or group are described and usually discussed in relation to the toxins involved in the pathology. Morphological and physiological characteristics of the organisms are described. Finally, the toxins produced by each organism are listed, with a presentation of their biological activities and physical and biochemical characteristics. The complete amino acid sequences for some are known, and some of the genes have been cloned. The term toxin is used loosely to include the various antigenic protein products of these organisms with biological and serological activities which have served as distinguishing characteristics for differentiation and classification. Some of these factors are not truly toxic and have no known role in pathogenicity. Some of the interesting factors common to more than one species or group are the following: neurotoxins, lethal toxins, lecithinases, oxygen-labile hemolysins, binary toxins, and ADP-ribosyltransferases. Problems in bacterial nomenclature and designation of biologically active factors are noted.

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