A novel reverse lipase toxin substrate of the Staphylococcus aureus type VII secretion system
Year: 2026
Type: article
Abstract: The type VII secretion system (T7SS) is found in many Gram-positive bacteria and secretes toxins with antibacterial activity. Most characterised substrates have an N-terminal LXG domain that interacts with other helical partner proteins to form a composite T7SS targeting signal. Here we describe only the second substrate family to have a reverse domain arrangement. We show that TslM has a C-terminal LXG-like domain and an N-terminal lipase domain that has phospholipase activity. Secretion of TslM requires a single helical partner protein that binds to the TslM C-terminus, and its toxic activity is neutralised by a distinct family of membrane proteins. Genome analysis reveals that Staphylococcus aureus strains have the capacity to encode up to seven paralogous copies of this toxin family. Taken together our findings show that lipases are an important component of the staphylococcal T7SS toxin arsenal, and that toxins with a reverse domain arrangement are more widespread than previously appreciated.
Source: microLife
Language: English
Subfield: Infectious Diseases
Field: Medicine
Domain: Health Sciences
Open Access status: gold
Estimated APC paid: $3,297
Awards: G1066391547, The Staphylococcus aureus Type VII secretion system and its role in bacterial antagonism, NLD (Newcastle-Liverpool-Durham) Doctoral Training Partnership 3, The Staphylococcus aureus Type VII secretion system and its role in bacterial antagonism, Newcastle Liverpool Durham BBSRC DTP2, G6868616705, G7483351365, G8038707669
OpenAlex ID: W7204156487