Pathogenesis of Staphylococcus aureus in Humans

Lu, Thea; DeLeo, Frank R.

doi:10.1002/9781118644843.ch39

Cited by 5 publications

(3 citation statements)

References 565 publications

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“…Based on the latest news, approximately 11–21 million cases and 128,000–161,000 typhoid-related deaths occur annually worldwide ( 21 , 22 ). Another common main cause of human infection is Staphylococcus aureus ( 23 ). All strains of Staphylococcus aureus can produce compounds that may attack innate and adaptive immunity ( 24 ).…”

Section: Discussionmentioning

confidence: 99%

Antibacterial activity of endosymbiotic bacterial compound from Pheretima sp. earthworms inhibit the growth of Salmonella Typhi and Staphylococcus aureus: in vitro and in silico approach

Husain¹,

Wardhani²

2021

IJM

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Background and Objectives: Earthworms coexist with various pathogenic microorganisms; thus, their immunity mecha- nisms have developed through a long process of adaptation, including through endogenous bacterial symbionts. This study aims to identify earthworm endosymbiont bacteria compounds and their antibacterial activity through an in vitro approach supported by an in silico approach. Materials and Methods: This research was conducted using the in vitro inhibition test through agar diffusion and the in silico test using molecular docking applications, namely, PyRx and Way2Drugs Prediction of Activity Spectra for Substances (PASS). Results: The in vitro results showed a potent inhibition activity with a clear zone diameter of 21.75 and 15.5 mm for Staph- ylococcus aureus and Salmonella Typhi, respectively. These results are supported by chromatography and in silico tests, which showed that several compounds in endosymbiotic bacteria, cyclo (phenylalanyl-prolyl) and sedanolide, have high binding affinity values with several antibiotic-related target proteins in both pathogenic bacteria. Cyclo (phenylalanyl-prolyl) has the highest binding affinity of -6.0 to dihydropteroate synthase, -8.2 to topoisomerase, and -8.2 to the outer membrane, whereas sedanolide has the highest binding affinity to DNA gyrase with approximately -7.3. This antibiotic activity was also clarified through the Way2Drugs PASS application. Conclusion: Ten active compounds of endosymbiont bacteria, Cyclo (phenylalanyl-prolyl) and sedanolide were potential candidates for antibacterial compounds based on the inhibition test of the agar diffusion method and the results of reverse docking and Way2Drugs PASS.

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Section: Discussionmentioning

confidence: 99%

Antibacterial activity of endosymbiotic bacterial compound from Pheretima sp. earthworms inhibit the growth of Salmonella Typhi and Staphylococcus aureus: in vitro and in silico approach

Husain¹,

Wardhani²

2021

IJM

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“…Staphylococcus aureus is a highly virulent pathogen that settles different sites of the body, including skin and mucous membranes of the nasopharynx, Gastrointestinal tract GIT and perineum and the genitourinary tracts (den et al,2013). It can be a cause of range of minor to critical infections in nearly most body tissues, chiefly in immune-deficient people like pneumonia, bloodstream infections and septic shock, skin and softtissue infections, burns and surgical-site infections in addition to endocarditis and many numerous infections (Lu & DeLeo, 2015). It can cause extensive series of human and animals' infectious diseases that carry a weighty reverse influence on public health.…”

Section: Introductionmentioning

confidence: 99%

Staphylococcal variable number tandem repeat (VNTR)-spa genotyping and their role in phylogenic study

Gazi

Al-shukri

Chabuck

et al. 2023

JANS

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Staphylococcus aureus protein A is considered a vital virulence element determinant of its pathogenicity. Its sequence diversity aids in staphylococcal typing and phylogeny. The present study aimed to study the genotyping method for S. aureus isolates by applying Spa typing (variable number tandem repeat) and their role in the phylogenic study. Twenty S. aureus isolates were achieved from various clinical isolates and subjected for complete identification and diagnosis. Later on, these isolates were subjected to DNA extraction and PCR for amplification and sequencing of SPA gene. Spa genotyping showed that out of 20 isolates and their amplified spa gene, 8 different types among the 18/20 isolates were detected and 2/20 isolates could not be typed, as the most commonly observed Spa were t304 (35%), t491 (15%) followed by t078 and t059 (10%). Finally, depending on the bacterial phylogenetic relationships, S. aureus isolates were categorized into 2 clades. The first one contained 18 isolates and the second one contained 2 isolates. Most Spa types were included in clade A (18 isolates) whereas only 2 isolates were involved in clade B. The isolates in clade A were grouped into 3 different groups established on the dissimilarity in tandem repeats of the Spa gene. Cluster 1 contained t304, t078, t044 Spa types, cluster 2 contained t059, t4870 and t386 Spa types and cluster 3 contained t491 and t091 Spa types. Clade B contained 2 Spa types (unknown). The utility of the present work is the application of repetitive tandem repeats within the spa gene for phylogenetic analysis of Staph aureus clinical isolates.

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“…Staphylococcus aureus is a Gram-positive bacterium that resides in the anterior nares of approximately one-third of the population. Diseases caused by S. aureus range in severity from minor skin and soft tissue infections, to life-threatening infections such as endocarditis, necrotizing fasciitis, and sepsis [1]. This incredible diversity in diseases is largely due to the multitude of virulence factors that S. aureus produces, such as exoenzymes that assist in the degradation of host molecules, adhesins that aid in attachment to surfaces, and toxins that lyse host cells [2,3,4,5].…”

Section: Introductionmentioning

confidence: 99%

Novel Regulation of Alpha-Toxin and the Phenol-Soluble Modulins by Peptidyl-Prolyl cis/trans Isomerase Enzymes in Staphylococcus aureus

Keogh

Zapf

Trzeciak

et al. 2019

Toxins

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Peptidyl-prolyl cis/trans isomerases (PPIases) are enzymes that catalyze the cis-to-trans isomerization around proline bonds, allowing proteins to fold into their correct confirmation. Previously, we identified two PPIase enzymes in Staphylococcus aureus (PpiB and PrsA) that are involved in the regulation of virulence determinants and have shown that PpiB contributes to S. aureus virulence in a murine abscess model of infection. Here, we further examine the role of these PPIases in S. aureus virulence and, in particular, their regulation of hemolytic toxins. Using murine abscess and systemic models of infection, we show that a ppiB mutant in a USA300 background is attenuated for virulence but that a prsA mutant is not. Deletion of the ppiB gene leads to decreased bacterial survival in macrophages and nasal epithelial cells, while there is no significant difference when prsA is deleted. Analysis of culture supernatants reveals that a ppiB mutant strain has reduced levels of the phenol-soluble modulins and that both ppiB and prsA mutants have reduced alpha-toxin activity. Finally, we perform immunoprecipitation to identify cellular targets of PpiB and PrsA. Results suggest a novel role for PpiB in S. aureus protein secretion. Collectively, our results demonstrate that PpiB and PrsA influence S. aureus toxins via distinct mechanisms, and that PpiB but not PrsA contributes to disease.

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Pathogenesis of Staphylococcus aureus in Humans

Cited by 5 publications

References 565 publications

Antibacterial activity of endosymbiotic bacterial compound from Pheretima sp. earthworms inhibit the growth of Salmonella Typhi and Staphylococcus aureus: in vitro and in silico approach

Antibacterial activity of endosymbiotic bacterial compound from Pheretima sp. earthworms inhibit the growth of Salmonella Typhi and Staphylococcus aureus: in vitro and in silico approach

Staphylococcal variable number tandem repeat (VNTR)-spa genotyping and their role in phylogenic study

Novel Regulation of Alpha-Toxin and the Phenol-Soluble Modulins by Peptidyl-Prolyl cis/trans Isomerase Enzymes in Staphylococcus aureus

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