DocumentCode
3340883
Title
Notice of Retraction
Expression and Antibody Production of the NP1 and VP1u Gene from Human Bocavirus
Author
Jinfeng Ouyang ; Jie Xiao ; Hu Han ; Jingjing Li ; Bin Sun ; Sheng Ding ; Yongbo Yang ; Yi Li
Author_Institution
Inst. of Entomology, Hua Zhong Normal Univ., Wuhan, China
fYear
2011
fDate
10-12 May 2011
Firstpage
1
Lastpage
4
Abstract
Notice of Retraction
After careful and considered review of the content of this paper by a duly constituted expert committee, this paper has been found to be in violation of IEEE´s Publication Principles.
We hereby retract the content of this paper. Reasonable effort should be made to remove all past references to this paper.
The presenting author of this paper has the option to appeal this decision by contacting TPII@ieee.org.
The nonstructural gene NP1 and structural gene VP1u of human Bocavirus, a newly found etiological parvovirus of lower respiratory tract infection in children, were cloned and expressed as MBP-NP1 and MBP-VP1u fusion proteins in Escherichia coli. The recombinant proteins were purified by Amylose affinity chromatography and then cleaved by the Factor Xa to remove the tag. MBP Tag-free proteins were used to immunize the New Zealand white rabbit or white mouse respectively to make antibodies, which along with the purified proteins provide reliable tools for diagnosis and the study of the virus.
After careful and considered review of the content of this paper by a duly constituted expert committee, this paper has been found to be in violation of IEEE´s Publication Principles.
We hereby retract the content of this paper. Reasonable effort should be made to remove all past references to this paper.
The presenting author of this paper has the option to appeal this decision by contacting TPII@ieee.org.
The nonstructural gene NP1 and structural gene VP1u of human Bocavirus, a newly found etiological parvovirus of lower respiratory tract infection in children, were cloned and expressed as MBP-NP1 and MBP-VP1u fusion proteins in Escherichia coli. The recombinant proteins were purified by Amylose affinity chromatography and then cleaved by the Factor Xa to remove the tag. MBP Tag-free proteins were used to immunize the New Zealand white rabbit or white mouse respectively to make antibodies, which along with the purified proteins provide reliable tools for diagnosis and the study of the virus.
Keywords
biochemistry; cellular biophysics; chromatography; diseases; enzymes; genetics; genomics; microorganisms; molecular biophysics; molecular configurations; patient diagnosis; physiological models; MBP tag-free proteins; amylose affinity chromatography; antibodies; antibody production; escherichia coli; etiological parvovirus; fusion proteins; gene cloning; gene expression; human bocavirus; immunization; lower respiratory tract infection; nonstructural gene NP1; patient diagnosis; recombinant proteins; structural gene VP1u; white mouse model; white rabbit model; DNA; Humans; Mice; Production; Proteins; Purification; Rabbits;
fLanguage
English
Publisher
ieee
Conference_Titel
Bioinformatics and Biomedical Engineering, (iCBBE) 2011 5th International Conference on
Conference_Location
Wuhan
ISSN
2151-7614
Print_ISBN
978-1-4244-5088-6
Type
conf
DOI
10.1109/icbbe.2011.5781266
Filename
5781266
Link To Document