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Contributor
Jesus Segovia
Digital Publisher
Digital Commons at St. Mary's University
Publication Date
Spring 2025
Keywords
Mycoplasma pneumoniae
Description
Mycoplasma pneumoniae is a microorganism that causes respiratory infection ranging in acuteness. Its connection to developing pneumonia is most widely known and this causes misleading assumptions for M. pneumoniae to be a mild infection.1 However, it is possible for many cases to arise in small populations or even spread epidemically.² M. pneumoniae is also known to cause extrapulmonary infections ranging in a wide variety of symptoms, such as skin rashes, psychological disorders, and arthritis.3 The mechanism by which M. pneumoniae can cause such diverse disease is unknown and still under investigation. Looking further into the functions of this pathogen would provide deeper understanding and potentially ways to decrease infection.
It is speculated that M. pneumoniae is unique from other mycoplasmas as it generates an exotoxin that enter host cells during infection. This exotoxin is called Community Community-Acquired Respiratory Distress Syndrome or CARDS Toxin. CARDS Toxin is a protein that consists of three known subunits or domains, labeled D1, D2, and D3. It is known that D1, or the N-terminal, has ADP-phosphorylating activity once the toxin enters a cell.1 Yet, the roles of D2 and D3, or the C-terminal, are still undetermined. It is speculated that the C-terminal triggers harmful vacuole production and disconnects from D1 once in the cell. The uncertainty of these domains gives rise to concerning questions for the understanding of M. pneumoniae and the effects it can have on intracellular mechanisms as a whole.
We hypothesize that mutating CARDS toxin DNA at the 132nd amino acid, changing Glutamine (E) to Alanine (A), would hinder the toxin’s ability to perform ADPPhosphorylation. Amplification of the N- and C- terminals separately would allow the mutation to be developed, and generating an ADP-ribosylating-deficient mutant of CARDS toxin will help us better determine if the mechanism of vacuolization is independent of ADP-ribosylation
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1 page
City
San Antonio, Texas
Creative Commons License
This work is licensed under a Creative Commons Attribution-NonCommercial-No Derivative Works 4.0 International License.
