Skip to main page content
U.S. flag

An official website of the United States government

Dot gov

The .gov means it’s official.
Federal government websites often end in .gov or .mil. Before sharing sensitive information, make sure you’re on a federal government site.

Https

The site is secure.
The https:// ensures that you are connecting to the official website and that any information you provide is encrypted and transmitted securely.

Access keys NCBI Homepage MyNCBI Homepage Main Content Main Navigation
Review
. 2016 Oct;12(5):553-559.
doi: 10.1007/s12015-016-9670-8.

Cellular GFP Toxicity and Immunogenicity: Potential Confounders in in Vivo Cell Tracking Experiments

Affiliations
Review

Cellular GFP Toxicity and Immunogenicity: Potential Confounders in in Vivo Cell Tracking Experiments

Amir Mehdi Ansari et al. Stem Cell Rev Rep. 2016 Oct.

Abstract

Green Fluorescent protein (GFP), used as a cellular tag, provides researchers with a valuable method of measuring gene expression and cell tracking. However, there is evidence to suggest that the immunogenicity and cytotoxicity of GFP potentially confounds the interpretation of in vivo experimental data. Studies have shown that GFP expression can deteriorate over time as GFP tagged cells are prone to death. Therefore, the cells that were originally marked with GFP do not survive and cannot be accurately traced over time. This review will present current evidence for the immunogenicity and cytotoxicity of GFP in in vivo studies by characterizing these responses.

Keywords: Cell death; Cytotoxicity; Green fluorescent protein (GFP); Immunogenicity; In vivo cell tracking; Reporter gene.

PubMed Disclaimer

Conflict of interest statement

The authors of this manuscript do not indicate any conflict of interest.

Figures

Fig. 1
Fig. 1
Molecular Structure of GFP. The tertiary structure of GFP is a beta barrel structure made up of 11 antiparallel β-strands (1) and 6 center-positioned alpha helices (2). Interrupting the stranded alpha helix, there are short helical loops on the ends of the cylindrical structure (3). A covalently bonded chromophore, 4-(p-hydroxybenzylidene) imidazolidin-5-one, is located and protected at the center of the structure (4)

References

    1. Shimomura O, Johnson FH, Saiga Y. Extraction, purification and properties of aequorin, a bioluminescent protein from the luminous hydromedusan, Aequorea. Journal of Cellular and Comparative Physiology. 1962;59:223–239. doi: 10.1002/jcp.1030590302. - DOI - PubMed
    1. Morise H, Shimomura O, Johnson FH, Winant J. Intermolecular energy transfer in the bioluminescent system of Aequorea. Biochemistry. 1974;13(12):2656–2662. doi: 10.1021/bi00709a028. - DOI - PubMed
    1. Shimomura O. Structure of the chromophore of Aequorea green fluorescent protein. FEBS Letters. 1979;104(2):220–222. doi: 10.1016/0014-5793(79)80818-2. - DOI
    1. Prasher DC, Eckenrode VK, Ward WW, Prendergast FG, Cormier MJ. Primary structure of the Aequorea victoria green-fluorescent protein. Gene. 1992;111(2):229–233. doi: 10.1016/0378-1119(92)90691-H. - DOI - PubMed
    1. Chalfie M, Tu Y, Euskirchen G, Ward WW, Prasher DC. Green fluorescent protein as a marker for gene expression. Science. 1994;263(5148):802–805. doi: 10.1126/science.8303295. - DOI - PubMed

MeSH terms

Substances