Dermal Filler Hypersensitivity Post-COVID-19 Illness: Case Series and Literature Review.

OBJECTIVE: To report two cases of dermal filler hypersensitivity post-COVID-19 illness and review the literature. METHODS: A literature review was performed. Data were extracted from the articles: the author, year of publication, age and sex of the patient, filler substance, injection site, symptoms and signs, onset time, diagnostic results, treatment, and prognosis. RESULTS: Six cases from six literatures were included in the review. All of them were female and were confirmed infected with COVID-19. Five of them received hyaluronic acid injection and one patient received polyacrylamide. Time after injection ranged from 8 months to 9 years. Onset of symptoms ranged from two to four weeks post-infection. The clinical manifestations included swelling, edema, induration, erythema, and tenderness. The site where the symptoms appeared was the injection site, and symptoms appeared at each injection site at the same time, including cheeks, periocular area, and lips. CONCLUSION: Dermal filler hypersensitivity may occur post-COVID-19 illness. A detailed history and clinical examination can help confirm the diagnosis. LEVEL OF EVIDENCE V: This journal requires that authors assign a level of evidence to each article. For a full description of these Evidence-Based Medicine ratings, please refer to the Table of Contents or the online Instructions to Authors www.springer.com/00266 .

Characterization of 17ß-hydroxysteroid dehydrogenase and regulators involved in estrogen degradation in Pseudomonas putida SJTE-1.

In bacteria, the enzyme catalyzing the transformation of 17ß-estradiol is considered the key enzyme for its metabolism, whose enzymatic activity and regulatory network influence the biodegradation efficiency of this typical estrogen. In this work, a novel 17ß-hydroxysteroid dehydrogenase (17ß-HSD) was characterized from the estrogen-degrading strain Pseudomonas putida SJTE-1, and two regulators were identified. This 17ß-HSD, a member of the short-chain dehydrogenase/reductase (SDR) superfamily, could be induced by 17ß-estradiol and catalyzed the oxidization reaction at the C17 site of 17ß-estradiol efficiently. Its Km value was 0.068 mM, and its Vmax value was 56.26 µmol/min/mg; over 98% of 17ß-estradiol was oxidized into estrone in 5 min, indicating higher efficiency than other reported bacterial 17ß-HSDs. Furthermore, two genes (crgA and oxyR) adjacent to 17ß-hsd were studied which encoded the potential CrgA and OxyR regulators. Overexpression of crgA could enhance the transcription of 17ß-hsd, while that of oxyR resulted in the opposite effect. They could bind to the specific and different sites in the promoter region of 17ß-hsd gene directly, and binding of OxyR could be released by 17ß-estradiol. OxyR repressed the expression of 17ß-hsd by its specific binding to the conserved motif of GATA-N9-TATC, while CrgA activated the expression of this gene through its binding to the motif of T-N11-A. Therefore, this 17ß-HSD transformed 17ß-estradiol efficiently and the two regulators regulated its expression directly. This work could promote the study of the enzymatic mechanism and regulatory network of the estrogen biodegradation pathway in bacteria.

One 3-oxoacyl-(acyl-Carrier-protein) reductase functions as 17ß-hydroxysteroid dehydrogenase in the estrogen-degrading Pseudomonas putida SJTE-1.

Pseudomonas putida SJTE-1 can utilize 17ß-estradiol (E2) as its carbon source, while the enzymes for E2 transformation in this strain is still unclear. 17ß-hydroxysteroid dehydrogenases (17ß-HSD) can catalyze the reduction/oxidation at C17 site of steroid hormone specifically, critical for steroid transformation. Here a novel 3-oxoacyl-(acyl-carrier protein) (ACP) reductase (ANI02794.1) was identified as it could bß-estradiol, and was proved to be capable of functioning as 17ß-HSD. Sequences alignment showed it contained the two consensus regions and the conserved residues of short-chain dehydrogenase/reductase (SDR). Its encoding gene was cloned and over-expressed in Escherichia coli BL21(DE3) strain, and the recombinant protein was purified by the metal-ion affinity chromatography with the yield of 18 mg/L culture. HPLC (High Performance Liquid Chromatography) detection showed this enzyme could convert 17ß-estradiol into estrone using NAD+ as cofactor. Its Km value was 0.082 mM and its Vmax value was 0.81 mM/s; its transformation efficiency of 17ß-estradiol into estrone was over 96.6% in five minutes. Its optimal temperature was 37 °C and optimal was pH 9.0; the divalent ions had different effects on the enzymatic activity. In conclusion, this 3-oxoacyl-ACP reductase functioned as 17ß-HSD in P. putida SJTE-1 and played important role in its estrogen metabolism.

iTRAQ-based quantitative proteomic analysis of the global response to 17ß-estradiol in estrogen-degradation strain Pseudomonas putida SJTE-1.

Microorganism degradation is efficient to remove the steroid hormones like 17ß-estradiol (E2); but their degradation mechanism and metabolic network to these chemicals are still not very clear. Here the global responses of the estrogen-degradation strain Pseudomonas putida SJTE-1 to 17ß-estradiol and glucose were analyzed and compared using the iTRAQ (isobaric tags for relative and absolute quantization) strategy combined with LC-MS/MS (liquid chromatography-tandem mass spectrometry). 78 proteins were identified with significant changes in expression; 45 proteins and 33 proteins were up-regulated and down-regulated, respectively. These proteins were mainly involved in the processes of stress response, energy metabolism, transportation, chemotaxis and cell motility, and carbon metabolism, considered probably responding to 17ß-estradiol and playing a role in its metabolism. The up-regulated proteins in electron transfer, energy generation and transport systems were thought crucial for efficient uptake, translocation and transformation of 17ß-estradiol. The over-expression of carbon metabolism proteins indicated cells may activate related pathway members to utilize 17ß-estradiol. Meanwhile, proteins functioning in glucose capture and metabolism were mostly down-regulated. These findings provide important clues to reveal the 17ß-estradiol degradation mechanism in P. putida and promote its bioremediation applications.