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The guаnidinium сhlоridе is used to сurе yеаst сеlls of аmylоid рriоns

A Literature Review

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Various protein-protein interactions have been confirmed to cause infections in cells. When this occurs in yeast cells, the protein chains therein significantly alter their physical form and cause the entire cell to malfunction. The cell is thus said to have developed ‘amyloid prions’, a condition considered being a great health hazard (Stephens et al, 2008). The present literature review explores the curing ability of guanidinium chloride of yeast cells from amyloid prions. To do this, the author presents an overview of how amyloid prions develops in yeast cells and how guanidinium chloride has been used in curing prions before making the concluding remarks.


Extant literature has doubtlessly demonstrated that amyloid prions occur in cells due to protein-protein interactions, adversely affecting the structure of polypeptide chains of the protein (Moseley and Goode, 2006). When this happens, the cell loses its potency and is hence unable to function properly. This condition is characteristic of a prion, an infectious protein present in both mammals and fungi (Cooper et al, 2009). According to works carried out by Bowers and Stevens (2005) and Ness and associates (2002) in studying the physiology of the yeast cell, prions have been reported to be ‘self-propagating agents’ that are very sensitive to temperature values. In fact, Rajmohan and partners (2009) note that high temperatures favor the propagation and maintenance of prions in yeast. This argument is further confirmed by results forwarded by Boisvert and colleagues (2007) claiming that most yeast cell prions occurred at temperature values of above 24°C.

In the same vein, Marina and Giuseppe (2012) illustrate that prions are capable of developing intermittently and thus emitting their injurious agents in small doses. This characteristic makes prions extremely lethal, particularly if they are originating from animals. Numerous explanations have been forwarded to support this argument. Firstly, prions of animal nature are indicated to produce multiple strains that cause infectious reactions in humans. Secondly, Fernandez-Martinez and Rout (2009) argue that prions found in yeast cells result in more stable strains capable of producing ‘self-replicating hereditary particles’, which help in maintaining their potency (Marina and Giuseppe, 2012). Finally, Rajmohan and friends (2009) underscore the dangerous nature of yeast prions. In their views, yeast prions are capable of influencing the appearance of other life-threatening prions upon their successful transmission. In view of these highlights, it becomes emphatic to come up with a concrete cure for amyloid prions in yeast cells.


Arguments have been rife in underlying the significance of guanidinium chloride in alleviating common problems resulting from protein-protein interactions. As indicated in the works of Valerie and associates (2004), guanidinium chloride is capable of denaturing proteins in many ways. This action by extension is considered by Ness et al (2002) to constitute an effective ‘cure’ for prion positive cells if administered in the right concentrations. Based on this argument therefore, cells that had earlier indicated to be ‘prion positive’ immediately changed to ‘prion negative’ status after the right doses of guanidinium chloride were administered (Ness et al, 2002). In trying to explain the working mechanism of guanidinium chloride in this aspect, Rajmohan et al (2009) adds that guanidinium chloride blocks the action of the factor responsible for the production and propagation of prions in cells. Similarly, observations by Valerie and partners (2004) reveal that guanidinium chloride is responsible for minimizing the negative effects of defective nervous system. It does this by ensuring that enough acetylcholine is released to facilitate transmission of an impulse across the synapse, forestalling the risk of muscle cramps.

Apart from the foregoing indications, numerous reports show that guanidinium chloride is capable of preventing the production of prions by its action on temperature. Since production and effective propagation of prions in cells is promoted by intense temperatures, guanidinium chloride’s ability to ‘impair heat shock resistance’ as noted by Cooper et al (2009) is enough to forestall this occurrence. Moreover, continued additions of small quantities of guanidinium chloride to yeast medium under conditions of controlled temperature values results in total elimination of prion-positive cells. Further findings in extant literature strongly suggest that guanidinium chloride cures amyloid prions in yeast cells by causing a disturbance of the enzyme ATPase of the factor responsible for the production, propagation and thermo-tolerance of prions (Valerie et al, 2004).

Based on the accessed literature in this review, it is clearly illustrated that the use of guanidinium chloride to cure yeast amyloid prions has been effective, but not without some side effects. According to Moseley and Goode (2006), continued use of guanidinium chloride has led to ‘increased peristalsis, diarrhea and fatal bone-marrow suppression’ among other symptoms. These negative indications have been reported to be dose-related, particularly when an overdose is sustained longer than necessary.


Following the arguments presented throughout this discourse, guanidinium chloride has been demonstrated to be instrumental in arresting adverse effects of amyloid prions in yeast cells. This confirms the hypothesis formulated at the inception of this review that: “the guаnidinium сhlоridе is used to сurе yеаst сеlls of аmylоid рriоns”. This is achieved through a number ways clearly described in this review.


Boisvert, F. M., Lamond, A. I., van Koningsbruggen, S. and Navascues, J. (2007) The

multifunctional nucleolus. Nature Reviews Molecular Cell Biology, 8, 574–585.

Bowers, K. and Stevens, T. H. (2005) Protein transport from the late Golgi to the

vacuole in the yeast Saccharomyces cerevisiae. Biochemica et Biophysica Acta, 1744, 438–454 (review).

Cooper, J. A., Stuchell-Brereton, M. D., and Moore, J. K. (2009) Function of dynein in

budding yeast: mitotic spindle positioning in a polarized cell. Cell Motility and the Cytoskeleton, 66, 546–555.

Fernandez-Martinez, J. and Rout, M. P. (2009) Nuclear pore complex biogenesis.

Current Opinion in Cell Biology, 21, 603–612.

Marina, N. and Giuseppe, R. (2012) Non-muscle myosins and the podocyte. Clinical

Kidney Journal, Volume 5, Issue 2, Pp. 94-101.

Moseley, J. B. and Goode, B. L. (2006) The yeast actin cytoskeleton: from cellular

function to biochemical mechanism. Microbiology and Molecular Biology Reviews, 70, 605–645.

Ness, F., Ferreira, P., Cox, B. S., and Tuite, M. F. (2002) Guanidine hydrochloride

inhibits the generation of prion “seeds” but not prion protein aggregation in yeast.

Rajmohan, R., Wong, M. H., Meng, L., Munn, A. L., and Thanabalu, T. (2009) Las17p-

Vrp1p but not Las17p-Arp2/3 interaction is important for actin patch polarization in yeast. Biochim Biophys Acta, 1793: 825-35.

Stephens, A. E., Gardiner, D. M., White, R. G., Munn, A. L., and Manners, J. M. (2008)

Phases of infection and gene expression of Fusarium graminearum during crown rot disease of wheat. Mol Plant Microbe Interact, 21, 1571-81.

Valerie, G., Klaus, R., Axel, I., Johannes, B., and Stefan, W. (2004) The Prion Curing

Agent Guanidinium Chloride Specifically Inhibits ATP Hydrolysis by Hsp104. The Journal of Biological Chemistry, 279, 7378-7383.

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