Role of the Sortase A in the Release of Cell-Wall Proteinase PrtS in the Growth Medium of <i>Streptococcus thermophilus</i> 4F44
Growth of the lactic acid bacterium <i>Streptococcus thermophilus</i> in milk depends on its capacity to hydrolyze proteins of this medium through its surface proteolytic activity. Thus, strains exhibiting the cell envelope proteinase (CEP) PrtS are able to grow in milk at high cellular...
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oai:doaj.org-article:afd0a01b163a48be9cde584709db5d0c2021-11-25T18:25:33ZRole of the Sortase A in the Release of Cell-Wall Proteinase PrtS in the Growth Medium of <i>Streptococcus thermophilus</i> 4F4410.3390/microorganisms91123802076-2607https://doaj.org/article/afd0a01b163a48be9cde584709db5d0c2021-11-01T00:00:00Zhttps://www.mdpi.com/2076-2607/9/11/2380https://doaj.org/toc/2076-2607Growth of the lactic acid bacterium <i>Streptococcus thermophilus</i> in milk depends on its capacity to hydrolyze proteins of this medium through its surface proteolytic activity. Thus, strains exhibiting the cell envelope proteinase (CEP) PrtS are able to grow in milk at high cellular density. Due to its LPNTG motif, which is possibly the substrate of the sortase A (SrtA), PrtS is anchored to the cell wall in most <i>S. thermophilus</i> strains. Conversely, a soluble extracellular PrtS activity has been reported in the strain 4F44. It corresponds, in fact, to a certain proportion of PrtS that is not anchored to the cell wall but rather is released in the growth medium. The main difference between PrtS of strain 4F44 (PrtS<sub>4F44</sub>) and other PrtS concerns the absence of a 32-residue imperfect duplication in the prodomain of the CEP, postulated as being required for the maturation and correct subsequent anchoring of PrtS. In fact, both mature (without the prodomain at the N-terminal extremity) and immature (with the prodomain) forms are found in the soluble PrtS<sub>4F44</sub> form along with an intact LPNTG at their C-terminal extremity. Investigations we present in this work show that (i) the imperfect duplication is not implied in PrtS maturation; (ii) the maturase PrtM is irrelevant in PrtS maturation which is probably automaturated; and (iii) SrtA allows for the PrtS anchoring in <i>S. thermophilus</i> but the SrtA of strain 4F44 (SrtA<sub>4F44</sub>) displays an altered activity.Ahoefa Ablavi AwussiEmeline RouxCatherine HumeauZeeshan HafeezBernard MaigretOun Ki ChangXavier LecomteGérard HumbertLaurent MicloMagali GenayClarisse PerrinAnnie Dary-MourotMDPI AGarticle<i>Streptococcus thermophilus</i>sortase Acell envelope proteinaseLPNTG motifcell wall-anchoringBiology (General)QH301-705.5ENMicroorganisms, Vol 9, Iss 2380, p 2380 (2021) |
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<i>Streptococcus thermophilus</i> sortase A cell envelope proteinase LPNTG motif cell wall-anchoring Biology (General) QH301-705.5 |
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<i>Streptococcus thermophilus</i> sortase A cell envelope proteinase LPNTG motif cell wall-anchoring Biology (General) QH301-705.5 Ahoefa Ablavi Awussi Emeline Roux Catherine Humeau Zeeshan Hafeez Bernard Maigret Oun Ki Chang Xavier Lecomte Gérard Humbert Laurent Miclo Magali Genay Clarisse Perrin Annie Dary-Mourot Role of the Sortase A in the Release of Cell-Wall Proteinase PrtS in the Growth Medium of <i>Streptococcus thermophilus</i> 4F44 |
description |
Growth of the lactic acid bacterium <i>Streptococcus thermophilus</i> in milk depends on its capacity to hydrolyze proteins of this medium through its surface proteolytic activity. Thus, strains exhibiting the cell envelope proteinase (CEP) PrtS are able to grow in milk at high cellular density. Due to its LPNTG motif, which is possibly the substrate of the sortase A (SrtA), PrtS is anchored to the cell wall in most <i>S. thermophilus</i> strains. Conversely, a soluble extracellular PrtS activity has been reported in the strain 4F44. It corresponds, in fact, to a certain proportion of PrtS that is not anchored to the cell wall but rather is released in the growth medium. The main difference between PrtS of strain 4F44 (PrtS<sub>4F44</sub>) and other PrtS concerns the absence of a 32-residue imperfect duplication in the prodomain of the CEP, postulated as being required for the maturation and correct subsequent anchoring of PrtS. In fact, both mature (without the prodomain at the N-terminal extremity) and immature (with the prodomain) forms are found in the soluble PrtS<sub>4F44</sub> form along with an intact LPNTG at their C-terminal extremity. Investigations we present in this work show that (i) the imperfect duplication is not implied in PrtS maturation; (ii) the maturase PrtM is irrelevant in PrtS maturation which is probably automaturated; and (iii) SrtA allows for the PrtS anchoring in <i>S. thermophilus</i> but the SrtA of strain 4F44 (SrtA<sub>4F44</sub>) displays an altered activity. |
format |
article |
author |
Ahoefa Ablavi Awussi Emeline Roux Catherine Humeau Zeeshan Hafeez Bernard Maigret Oun Ki Chang Xavier Lecomte Gérard Humbert Laurent Miclo Magali Genay Clarisse Perrin Annie Dary-Mourot |
author_facet |
Ahoefa Ablavi Awussi Emeline Roux Catherine Humeau Zeeshan Hafeez Bernard Maigret Oun Ki Chang Xavier Lecomte Gérard Humbert Laurent Miclo Magali Genay Clarisse Perrin Annie Dary-Mourot |
author_sort |
Ahoefa Ablavi Awussi |
title |
Role of the Sortase A in the Release of Cell-Wall Proteinase PrtS in the Growth Medium of <i>Streptococcus thermophilus</i> 4F44 |
title_short |
Role of the Sortase A in the Release of Cell-Wall Proteinase PrtS in the Growth Medium of <i>Streptococcus thermophilus</i> 4F44 |
title_full |
Role of the Sortase A in the Release of Cell-Wall Proteinase PrtS in the Growth Medium of <i>Streptococcus thermophilus</i> 4F44 |
title_fullStr |
Role of the Sortase A in the Release of Cell-Wall Proteinase PrtS in the Growth Medium of <i>Streptococcus thermophilus</i> 4F44 |
title_full_unstemmed |
Role of the Sortase A in the Release of Cell-Wall Proteinase PrtS in the Growth Medium of <i>Streptococcus thermophilus</i> 4F44 |
title_sort |
role of the sortase a in the release of cell-wall proteinase prts in the growth medium of <i>streptococcus thermophilus</i> 4f44 |
publisher |
MDPI AG |
publishDate |
2021 |
url |
https://doaj.org/article/afd0a01b163a48be9cde584709db5d0c |
work_keys_str_mv |
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