Other search tools

About this data

The publication data currently available has been vetted by Vanderbilt faculty, staff, administrators and trainees. The data itself is retrieved directly from NCBI's PubMed and is automatically updated on a weekly basis to ensure accuracy and completeness.

If you have any questions or comments, please contact us.

Results: 1 to 4 of 4

Publication Record

Connections

Corynebacterium accolens Releases Antipneumococcal Free Fatty Acids from Human Nostril and Skin Surface Triacylglycerols.
Bomar L, Brugger SD, Yost BH, Davies SS, Lemon KP
(2016) mBio 7: e01725-15
MeSH Terms: Anti-Bacterial Agents, Antibiosis, Carrier State, Child, Child, Preschool, Corynebacterium, Fatty Acids, Nonesterified, Humans, Hydrolysis, Infant, Microbiota, Nasal Cavity, Pneumococcal Infections, Skin, Streptococcus pneumoniae, Triglycerides, Triolein
Show Abstract · Added July 17, 2019
UNLABELLED - Bacterial interspecies interactions play clinically important roles in shaping microbial community composition. We observed that Corynebacterium spp. are overrepresented in children free of Streptococcus pneumoniae (pneumococcus), a common pediatric nasal colonizer and an important infectious agent. Corynebacterium accolens, a benign lipid-requiring species, inhibits pneumococcal growth during in vitro cocultivation on medium supplemented with human skin surface triacylglycerols (TAGs) that are likely present in the nostrils. This inhibition depends on LipS1, a TAG lipase necessary for C. accolens growth on TAGs such as triolein. We determined that C. accolens hydrolysis of triolein releases oleic acid, which inhibits pneumococcus, as do other free fatty acids (FFAs) that might be released by LipS1 from human skin surface TAGs. Our results support a model in which C. accolens hydrolyzes skin surface TAGS in vivo releasing antipneumococcal FFAs. These data indicate that C. accolens may play a beneficial role in sculpting the human microbiome.
IMPORTANCE - Little is known about how harmless Corynebacterium species that colonize the human nose and skin might impact pathogen colonization and proliferation at these sites. We show that Corynebacterium accolens, a common benign nasal bacterium, modifies its local habitat in vitro as it inhibits growth of Streptococcus pneumoniae by releasing antibacterial free fatty acids from host skin surface triacylglycerols. We further identify the primary C. accolens lipase required for this activity. We postulate a model in which higher numbers of C. accolens cells deter/limit S. pneumoniae nostril colonization, which might partly explain why children without S. pneumoniae colonization have higher levels of nasal Corynebacterium. This work narrows the gap between descriptive studies and the needed in-depth understanding of the molecular mechanisms of microbe-microbe interactions that help shape the human microbiome. It also lays the foundation for future in vivo studies to determine whether habitat modification by C. accolens could be promoted to control pathogen colonization.
Copyright © 2016 Bomar et al.
1 Communities
1 Members
0 Resources
MeSH Terms
Apolipoprotein A-V deficiency enhances chylomicron production in lymph fistula mice.
Zhang LS, Xu M, Yang Q, Ryan RO, Howles P, Tso P
(2015) Am J Physiol Gastrointest Liver Physiol 308: G634-42
MeSH Terms: Administration, Oral, Animals, Apolipoprotein A-V, Apolipoproteins, Cholesterol, Chylomicrons, Disease Models, Animal, Duodenum, Fistula, Intestinal Absorption, Lymph, Lymphatic Diseases, Lymphatic System, Male, Mice, Inbred C57BL, Mice, Knockout, Postprandial Period, Time Factors, Triolein, Up-Regulation
Show Abstract · Added August 24, 2015
Apolipoprotein A-V (apoA-V), a liver-synthesized apolipoprotein discovered in 2001, strongly modulates fasting plasma triglycerides (TG). Little is reported on the effect of apoA-V on postprandial plasma TG, an independent predictor for atherosclerosis. Overexpressing apoA-V in mice suppresses postprandial TG, but mechanisms focus on increased lipolysis or clearance of remnant particles. Unknown is whether apoA-V suppresses the absorption of dietary lipids by the gut. This study examines how apoA-V deficiency affects the steady-state absorption and lymphatic transport of dietary lipids in chow-fed mice. Using apoA-V knockout (KO, n = 8) and wild-type (WT, n = 8) lymph fistula mice, we analyzed the uptake and lymphatic transport of lipids during a continuous infusion of an emulsion containing [(3)H]triolein and [(14)C]cholesterol. ApoA-V KO mice showed a twofold increase in (3)H (P < 0.001) and a threefold increase in (14)C (P < 0.001) transport into the lymph compared with WT. The increased lymphatic transport was accompanied by a twofold reduction (P < 0.05) in mucosal (3)H, suggesting that apoA-V KO mice more rapidly secreted [(3)H]TG out of the mucosa into the lymph. ApoA-V KO mice also produced chylomicrons more rapidly than WT (P < 0.05), as measured by the transit time of [(14)C]oleic acid from the intestinal lumen to lymph. Interestingly, apoA-V KO mice produced a steadily increasing number of chylomicron particles over time, as measured by lymphatic apoB output. The data suggest that apoA-V suppresses the production of chylomicrons, playing a previously unknown role in lipid metabolism that may contribute to the postprandial hypertriglyceridemia associated with apoA-V deficiency.
Copyright © 2015 the American Physiological Society.
0 Communities
1 Members
0 Resources
20 MeSH Terms
Why does the gut choose apolipoprotein B48 but not B100 for chylomicron formation?
Lo CM, Nordskog BK, Nauli AM, Zheng S, Vonlehmden SB, Yang Q, Lee D, Swift LL, Davidson NO, Tso P
(2008) Am J Physiol Gastrointest Liver Physiol 294: G344-52
MeSH Terms: APOBEC-1 Deaminase, Animals, Apolipoprotein B-100, Apolipoprotein B-48, Apolipoproteins A, Carrier Proteins, Chylomicrons, Cytidine Deaminase, Dose-Response Relationship, Drug, Duodenum, Intestinal Absorption, Intestinal Mucosa, Intubation, Gastrointestinal, Lymph, Lymphatic System, Male, Mice, Mice, Inbred C57BL, Mice, Knockout, Models, Animal, Particle Size, Time Factors, Triolein
Show Abstract · Added December 10, 2013
Chylomicrons produced by the human gut contain apolipoprotein (apo) B48, whereas very-low-density lipoproteins made by the liver contain apo B100. To study how these molecules function during lipid absorption, we examined the process as it occurs in apobec-1 knockout mice (able to produce only apo B100; KO) and in wild-type mice (of which the normally functioning intestine makes apo B48, WT). Using the lymph fistula model, we studied the process of lipid absorption when animals were intraduodenally infused with a lipid emulsion (4 or 6 micromol/h of triolein). KO mice transported triacylglycerol (TG) as efficiently as WT mice when infused with the lower lipid dose; when infused with 6 micromol/h of triolein, however, KO mice transported significantly less TG to lymph than WT mice, leading to the accumulation of mucosal TG. Interestingly, the size of lipoprotein particles from both KO and WT mice were enlarged to chylomicron-size particles during absorption of the higher dose. These increased-size particles produced by KO mice were not associated with increased apo AIV secretion. However, we found that the gut of the KO mice secreted fewer apo B molecules to lymph (compared with WT), during both fasting and lipid infusion, leading us to conclude that the KO gut produced fewer numbers of TG-rich lipoproteins (including chylomicron) than the wild-type animals. The reduced apo B secretion in KO mice was not related to reduced microsomal triglyceride transfer protein lipid transfer activity. We propose that apo B48 is the preferred protein for the gut to coat chylomicrons to ensure efficient chylomicron formation and lipid absorption.
0 Communities
1 Members
0 Resources
23 MeSH Terms
Lysosomal hydrolysis of lipids in a cell culture model of smooth muscle foam cells.
Minor LK, Mahlberg FH, Jerome WG, Lewis JC, Rothblat GH, Glick JM
(1991) Exp Mol Pathol 54: 159-71
MeSH Terms: Ammonium Chloride, Animals, Aorta, Cells, Cultured, Chloroquine, Cholesterol Esters, Humans, Hydrolysis, Kinetics, Lipid Metabolism, Lipolysis, Lysosomes, Methylamines, Microscopy, Electron, Muscle, Smooth, Vascular, Rabbits, Skin, Triolein
Show Abstract · Added December 10, 2013
Rabbit aortic smooth muscle cells take up lipid droplets when they are presented using an inverted culture technique. These droplets were localized in secondary lysosomes as demonstrated by staining for acid phosphatase. Initially, 69% of the cell volume was occupied by lipid, and 94% of the lipid was in lysosomes. After a 24-hr clearance period, the cell volume occupied by lipid decreased to 53%, although there was no change in the fraction of cell lipid that was in lysosomes. To confirm that hydrolysis of droplet lipid was occurring in lysosomes, cultures were exposed to medium containing Sandoz 58-035, an inhibitor of acyl CoA:cholesterol acyl transferase, for 24 hr in the presence and absence of chloroquine, ammonium chloride, or methylamine. Although the hydrolysis of cholesteryl oleate was sensitive to these lysosomotropic agents, the hydrolysis of triolein was not. Using reconstituted LDL containing cholesteryl oleate and triolein, we demonstrated that the hydrolyses of cholesteryl oleate and triolein were equally sensitive to the lysosomotropic agents when the cells were not loaded with droplet lipid. However, in cells loaded with lipid, hydrolysis of LDL cholesteryl ester was sensitive to the lysosomotropic agents but hydrolysis of triolein was not. We therefore conclude that both droplet lipids were hydrolyzed in lysosomes, and we attribute the failure of the lysosomotropic agents to inhibit fully the hydrolysis of droplet triolein to the presence of a large mass of free fatty acids in the lysosome that maintains a sufficiently low pH to sustain the triglyceridase activity, but not the cholesteryl esterase activity, of the lysosomal acid lipase.
0 Communities
1 Members
0 Resources
18 MeSH Terms