Erratum for Le et al., Modulation of Adherence, Invasion, and Tumor Necrosis Factor Alpha Secretion during the Early Stages of Infection by Streptococcus pneumoniae ClpL

Le, Nhat Tu; Jeong, Hye Yoon; Kwon, Hyog Young; Ogunniyi, Abiodun D.; Paton, James C.; Pyo, Suhk Neung; Rhee, Dong Kwon

doi:10.1128/iai.03125-14

Infect Immun

2015

DOI: 10.1128/iai.03125-14

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Erratum for Le et al., Modulation of Adherence, Invasion, and Tumor Necrosis Factor Alpha Secretion during the Early Stages of Infection by Streptococcus pneumoniae ClpL

Nhat Tu Le

Hye Yoon Jeong

Hyog Young Kwon

et al.

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“…A S. mutans strain lacking a functional ClpL displays an acid-shock response and increased sensitivity to some antibiotics; however, its exact molecular function is currently unknown. S. mutans ClpL is highly homologous to its counterpart from Streptococcus pneumoniae and Streptococcus thermophilus . , ClpL is required for virulence expression and antibiotic resistance in S. pneumoniae , and in acid tolerance in S. thermophilus . Thus, it appears that the cellular function of ClpL is highly variable among streptococci.…”

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Significance of Individual Domains of ClpL: A Novel Chaperone from Streptococcus mutans

Jana

Biswas

2020

Biochemistry

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ClpL is a member of the HSP100 family of the AAA+ chaperone that is widely present in Grampositive but surprisingly absent in Gram-negative bacteria. ClpL is involved in various cellular processes including stress tolerance response, long-term survival, virulence, and antibiotic resistance. ClpL is poorly characterized and its molecular mechanisms of chaperone activity are largely unclear. Here, we biochemically characterized the ClpL protein from Streptococcus mutans, a dental pathogen, to understand its biological functions. ClpL harbors five domains: Ndomain, two nucleotide binding domains (NBD-1 and NBD-2), M-domain, and C-domain. NBD-1 and NBD-2 contain distinct Walker A and B motifs for ATP binding and hydrolysis, respectively. We found that ClpL predominantly exists as a trimer in solution; however, upon ATP binding, it rapidly forms a hexameric structure. To study structure-function activity, we constructed several substitution and deletion mutants. We found that mutations in Walker A and B motifs interfered with the ATP hydrolysis and oligomerization. Similarly, deletions of N-, M-, and C-domains abolished both the ATPase activity and oligomerization. Since we previously found that ClpL acts as a chaperone, we analyzed the chaperone activity. Surprisingly, we found that the NBD-2 mutants did not display any chaperone activity indicating the essentiality of ATP binding and hydrolysis by NBD-2 for chaperone. However, NBD-1 mutants showed chaperone activities, but the activities were variable depending on the nature of the mutations. Our results indicate that unlike other HSP100 family chaperones, ClpL is a novel chaperone that does not require any additional secondary chaperones for its activity.

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“…S. mutans ClpL is highly homologous to its counterpart from Streptococcus pneumoniae and Streptococcus thermophilus. 30,31 ClpL is required for virulence expression and antibiotic resistance in S. pneumoniae 30,32 and in acid tolerance in S. thermophilus. 31 Thus, it appears that the cellular function of ClpL is highly variable among streptococci.…”

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confidence: 99%

Significance of Individual Domains of ClpL: A Novel Chaperone from Streptococcus mutans

Jana

Biswas

2020

Biochemistry

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Erratum for Le et al., Modulation of Adherence, Invasion, and Tumor Necrosis Factor Alpha Secretion during the Early Stages of Infection by Streptococcus pneumoniae ClpL

Cited by 1 publication

References 0 publications

Significance of Individual Domains of ClpL: A Novel Chaperone from Streptococcus mutans

Significance of Individual Domains of ClpL: A Novel Chaperone from Streptococcus mutans

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