Characterization of a Swedish bovine isolate of Neospora caninum

1997 ◽  
Vol 83 (3) ◽  
pp. 214-219 ◽  
Author(s):  
S. Stenlund ◽  
C. Björkman ◽  
O. J. M. Holmdahl ◽  
H. Kindahl ◽  
A. Uggla
2009 ◽  
Vol 159 (1) ◽  
pp. 7-16 ◽  
Author(s):  
Silvia Rojo-Montejo ◽  
Esther Collantes-Fernández ◽  
Javier Regidor-Cerrillo ◽  
Gema Álvarez-García ◽  
Virginia Marugan-Hernández ◽  
...  

Parasitology ◽  
2012 ◽  
Vol 139 (8) ◽  
pp. 998-1004 ◽  
Author(s):  
X. CUI ◽  
T. LEI ◽  
D. Y. YANG ◽  
P. HAO ◽  
Q. LIU

SUMMARYImmune mapped protein 1 (IMP1) is a newly discovered protein in Eimeria maxima. It is recognized as a potential vaccine candidate against E. maxima and a highly conserved protein in apicomplexan parasites. Although the Neospora caninum IMP1 (NcIMP1) orthologue of E. maxima IMP1 was predicted in the N. caninum genome, it was still not identified and characterized. In this study, cDNA sequence encoding NcIMP1 was cloned by RT-PCR from RNA isolated from Nc1 tachyzoites. NcIMP1 was encoded by an open reading frame of 1182 bp, which encoded a protein of 393 amino acids with a predicted molecular weight of 42·9 kDa. Sequence analysis showed that there was neither a signal peptide nor a transmembrane region present in the NcIMP1 amino acid sequence. However, several kinds of functional protein motifs, including an N-myristoylation site and a palmitoylation site were predicted. Recombinant NcIMP1 (rNcIMP1) was expressed in Escherichia coli and then purified rNcIMP1 was used to prepare specific antisera in mice. Mouse polyclonal antibodies raised against the rNcIMP1 recognized an approximate 43 kDa native IMP1 protein. Immunofluorescence analysis showed that NcIMP1 was localized on the membrane of N. caninum tachyzoites. The N-myristoylation site and the palmitoylation site were found to contribute to the localization of NcIMP1. Furthermore, the rNcIMP1-specific antibodies could inhibit cell invasion by N. caninum tachyzoites in vitro. All the results indicate that NcIMP1 is likely to be a membrane protein of N. caninum and may be involved in parasite invasion.


2020 ◽  
Vol 280 ◽  
pp. 109091
Author(s):  
Marta García-Sánchez ◽  
Javier Moreno-Gonzalo ◽  
Marta González-Warleta ◽  
Mercedes Mezo ◽  
Luis Miguel Ortega-Mora ◽  
...  

2012 ◽  
Vol 187 (1-2) ◽  
pp. 28-35 ◽  
Author(s):  
Jigang Yin ◽  
Guanggang Qu ◽  
Lili Cao ◽  
Qichang Li ◽  
Raymond Fetterer ◽  
...  

2006 ◽  
Vol 135 (2-3) ◽  
pp. 130-141 ◽  
Author(s):  
S.W. Maley ◽  
D. Buxton ◽  
C.N. Macaldowie ◽  
I.E. Anderson ◽  
S.E. Wright ◽  
...  

Parasitology ◽  
2011 ◽  
Vol 138 (14) ◽  
pp. 1832-1842 ◽  
Author(s):  
V. RISCO-CASTILLO ◽  
V. MARUGÁN-HERNÁNDEZ ◽  
A. FERNÁNDEZ-GARCÍA ◽  
A. AGUADO-MARTÍNEZ ◽  
E. JIMÉNEZ-RUIZ ◽  
...  

SUMMARYHere we present the detection of a gene cluster forNeospora caninumsurface genes, similar to theToxoplasma gondiiSRS9 locus, and the cloning and characterization of the NcSRS9gene. PCR genome walking, using NcBSR4gene as a framework, allows the identification, upstream NcBSR4, of 2 sequences homologous to theSRS5and the Ubiquinol-cytochrome C reductase genes and, downstream NcBSR4, of an ORF of 1191 bp coding for a 396-amino acid polypeptide with 59% similarity to the TgSRS9 antigen. A putative 39-residue signal peptide was found at the NH2-terminus followed by a hydrophilic region, and a potential site for a glycosylphosphatidylinositol anchor at the COOH-terminus. A recombinant NcSRS9 protein was produced and was recognized on a Western blot by a low proportion of sera from a panel of naturally infected cows and calves. In addition, Western blot analysis using polyclonal anti-rNcSRS9 revealed stage-specific expression of NcSRS9 in bradyzoites but not in tachyzoites, and immunohistochemistry on brain from a congenitally infected calf showed NcSRS9 recognition in bradyzoites contained in tissue cysts. However, bradyzoite-specific expression of NcSRS9 could not be proven by immunofluorescence on bradyzoites obtainedin vitroand RT-PCR analysis showed no significant variations of NcSRS9transcripts duringin vitrotachyzoite-bradyzoite switch, probably due to incomplete maturity ofin vitrobradyzoites. Initial characterization of NcSRS9 in this study may lead to further studies for a better understanding ofN. caninumpersistence.


2002 ◽  
Vol 88 (4) ◽  
pp. 691
Author(s):  
Helen E. Quinn ◽  
Catherine M. D. Miller ◽  
Cheryl Ryce ◽  
Peter A. Windsor ◽  
John T. Ellis

2017 ◽  
Vol 26 (3) ◽  
pp. 253-279 ◽  
Author(s):  
Camila Koutsodontis Cerqueira-Cézar ◽  
Rafael Calero-Bernal ◽  
Jitender Prakash Dubey ◽  
Solange Maria Gennari

Abstract Neospora caninum is protozoan parasite with domestic and wild dogs, coyotes and grey wolves as the definitive hosts and many warm-blooded animals as intermediate hosts. It was cultivated and named in 1988. Neosporosis is a major disease of cattle and has no public health significance. Since 1990’s N. caninum has emerged as a major cause of abortion in cattle worldwide, including in Brazil. N. caninum also causes clinical infections in several other animal species. Considerable progress has been made in understanding the biology of N. caninum and there are more than 200 papers on this subject from Brazil. However, most of the reports on neosporosis from Brazil are serological surveys. Overall, little is known of clinical neosporosis in Brazil, particularly cattle. The few reports pertain to sporadic cases of abortion with no information on epidemics or storms of abortion. The objective of the present review is to summarize all reports from Brazil and suggest topic for further research, including prevalence of N. caninum oocysts in soil or in canine feces, and determining if there are additional definitive hosts, other than the domestic dog. There is need for a national survey in cattle using defined parameters. Future researches should focus on molecular characterization of N. caninum strains, possibility of vaccine production and relationship between wildlife and livestock epidemiology.


2004 ◽  
Vol 90 (3) ◽  
pp. 579-583 ◽  
Author(s):  
Esther Collantes-Fernández ◽  
Gema Álvarez-García ◽  
Valentín Pérez-Pérez ◽  
Juana Pereira-Bueno ◽  
Luis Miguel Ortega-Mora

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