Rise of Antibiotic Resistance: Gonorrhea

<p><span style="font-size:11pt"><span style="line-height:115%"><span arial="" style="font-family:"><b>Abstract</b>: This case focuses on antibiotic use leading to strains of resistant bacteria that can no longer be treated with the same medications. It uses the example of bacterial resistance to antibiotics to show how small changes in protein structures can lead to differences in protein function, specifically through changes in interaction with small molecule drugs. The case begins with examining the CDC page on drug-resistant gonorrhea and the prevalence of strains resistant to at least one antibiotic. It uses pre-readings on mechanisms of antibiotic function and mechanisms of resistance to frame the molecular explorations, which examine cephalosporin-susceptible and cephalosporin-resistant penicillin binding proteins. This case relates visualization of protein structure to the fundamental concept of structure-function relationships, then ties this back to natural selection of heritable traits and microevolution in bacteria.</span></span></span></p> <p><span style="font-size:11pt"><span style="line-height:115%"><span arial="" style="font-family:"><b>Molecules explored</b>: The primary molecule studied is penicillin-binding protein (PBP2) from <i>Neisseria gonorrhoeae</i> alone or with cephalosporin ligands bound. </span></span></span></p>

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Publication Details

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Published
2025-09-19
DOI
https://doi.org/10.25334/hqf5-v395
Primary Topic
Geochemistry and Geologic Mapping
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article
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article

Rise of Antibiotic Resistance: Gonorrhea

QUBES
Geochemistry and Geologic Mapping
article

Rise of Antibiotic Resistance: Gonorrhea

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Abstract

<p><span style="font-size:11pt"><span style="line-height:115%"><span arial="" style="font-family:"><b>Abstract</b>: This case focuses on antibiotic use leading to strains of resistant bacteria that can no longer be treated with the same medications. It uses the example of bacterial resistance to antibiotics to show how small changes in protein structures can lead to differences in protein function, specifically through changes in interaction with small molecule drugs. The case begins with examining the CDC page on drug-resistant gonorrhea and the prevalence of strains resistant to at least one antibiotic. It uses pre-readings on mechanisms of antibiotic function and mechanisms of resistance to frame the molecular explorations, which examine cephalosporin-susceptible and cephalosporin-resistant penicillin binding proteins. This case relates visualization of protein structure to the fundamental concept of structure-function relationships, then ties this back to natural selection of heritable traits and microevolution in bacteria.</span></span></span></p> <p><span style="font-size:11pt"><span style="line-height:115%"><span arial="" style="font-family:"><b>Molecules explored</b>: The primary molecule studied is penicillin-binding protein (PBP2) from <i>Neisseria gonorrhoeae</i> alone or with cephalosporin ligands bound. </span></span></span></p>

QUBES
University of Washington Tacoma (US)
Openalex Percentile: Top 34%
Geochemistry and Geologic Mapping
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