Heat shock protein 60 from Klebsiella pneumoniae protects mononuclear cells from apoptotic cell death induced by dexamethasone

Ortega-Ortega, Yolanda; Garcı́a-Latorre, Ethel; Lezama, Ruth; Luna-Herrera, Julieta; Vega-López, Armando; Domínguez-López, María Lilia

doi:10.1016/j.micpath.2011.07.001

Cited by 2 publications

(2 citation statements)

References 43 publications

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“…However, this ability may be dependent on its adaptation to environmental conditions [ 95 , 96 ]. Bacteria, including Klebsiella , can produce heat shock proteins, such as chaperones of the heat shock protein (HSP) family, which enable them to survive extreme temperatures or temperatures outside of the range in which K. pneumoniae typically thrives [ 97 ]. Heat shock proteins (HSPs) are a group of highly conserved proteins that are expressed in response to stressful situations, such as heat.…”

Section: The Impact Of Cellular Homeostasis On K Pneumoniae...mentioning

confidence: 99%

“…Heat shock proteins (HSPs) are a group of highly conserved proteins that are expressed in response to stressful situations, such as heat. They play a crucial role in protecting proteins from potential damage, which directly affects homeostatic regulatory functions [ 97 ]. When interpreting the presence of HSP in these bacteria with a homeostatic approach, it is important to consider that many bacteria with pathogenic potential may transition from free-living saprophytic forms in the environment to ecosystems associated with organisms with homeostatic regulation.…”

Section: The Impact Of Cellular Homeostasis On K Pneumoniae...mentioning

confidence: 99%

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Relevance of the Adjuvant Effect between Cellular Homeostasis and Resistance to Antibiotics in Gram-Negative Bacteria with Pathogenic Capacity: A Study of Klebsiella pneumoniae

Rivera-Galindo,

Aguirre-Garrido,

Garza-Ramos

et al. 2024

Antibiotics

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Antibiotic resistance has become a global issue. The most significant risk is the acquisition of these mechanisms by pathogenic bacteria, which can have a severe clinical impact and pose a public health risk. This problem assumes that bacterial fitness is a constant phenomenon and should be approached from an evolutionary perspective to develop the most appropriate and effective strategies to contain the emergence of strains with pathogenic potential. Resistance mechanisms can be understood as adaptive processes to stressful conditions. This review examines the relevance of homeostatic regulatory mechanisms in antimicrobial resistance mechanisms. We focus on the interactions in the cellular physiology of pathogenic bacteria, particularly Gram-negative bacteria, and specifically Klebsiella pneumoniae. From a clinical research perspective, understanding these interactions is crucial for comprehensively understanding the phenomenon of resistance and developing more effective drugs and treatments to limit or attenuate bacterial sepsis, since the most conserved adjuvant phenomena in bacterial physiology has turned out to be more optimized and, therefore, more susceptible to alterations due to pharmacological action.

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Section: The Impact Of Cellular Homeostasis On K Pneumoniae...mentioning

confidence: 99%

Section: The Impact Of Cellular Homeostasis On K Pneumoniae...mentioning

confidence: 99%

Relevance of the Adjuvant Effect between Cellular Homeostasis and Resistance to Antibiotics in Gram-Negative Bacteria with Pathogenic Capacity: A Study of Klebsiella pneumoniae

Rivera-Galindo,

Aguirre-Garrido,

Garza-Ramos

et al. 2024

Antibiotics

View full text Add to dashboard Cite

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Chaperonin 60: a paradoxical, evolutionarily conserved protein family with multiple moonlighting functions

2013

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Chaperonin 60 is the prototypic molecular chaperone, an essential protein in eukaryotes and prokaryotes, whose sequence conservation provides an excellent basis for phylogenetic analysis. Escherichia coli chaperonin 60 (GroEL), the prototype of this family of proteins, has an established oligomeric-structure-based folding mechanism and a defined population of folding partners. However, there is a growing number of examples of chaperonin 60 proteins whose crystal structures and oligomeric composition are at variance with GroEL, suggesting that additional complexities in the protein-folding function of this protein should be expected. In addition, many organisms have multiple chaperonin 60 proteins, some of which have lost their protein-folding ability. It is emerging that this highly conserved protein has evolved a bewildering variety of additional biological functions - known as moonlighting functions - both within the cell and in the extracellular milieu. Indeed, in some organisms, it is these moonlighting functions that have been left after the loss of the protein-folding activity. This highlights the major paradox in the biology of chaperonin 60. This article reviews the relationship between the folding and non-folding (moonlighting) activities of the chaperonin 60 family and discusses current knowledge on their molecular evolution focusing on protein domains involved in the non-folding chaperonin functions in an attempt to understand the emerging biology of this evolutionarily ancient protein family.

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Heat shock protein 60 from Klebsiella pneumoniae protects mononuclear cells from apoptotic cell death induced by dexamethasone

Cited by 2 publications

References 43 publications

Relevance of the Adjuvant Effect between Cellular Homeostasis and Resistance to Antibiotics in Gram-Negative Bacteria with Pathogenic Capacity: A Study of Klebsiella pneumoniae

Relevance of the Adjuvant Effect between Cellular Homeostasis and Resistance to Antibiotics in Gram-Negative Bacteria with Pathogenic Capacity: A Study of Klebsiella pneumoniae

Chaperonin 60: a paradoxical, evolutionarily conserved protein family with multiple moonlighting functions

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