Human Serum Albumin Enhances the Hemolytic Activity of Vibrio vulnificus

Choi, Mihwa; Sun, Haibin; Park, Ra-Young; Bai, Young-Hoon; Chung, Yoon-Young; Kim, Choon-Mee; Shin, Sung‐Heui

doi:10.1248/bpb.29.180

Cited by 7 publications

(6 citation statements)

References 24 publications

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“…Previous studies have also shown that ApoE has a lipid-binding function, and the interaction with lipids induces a change in the conformation of the amino-terminal domain leading to alterations in function; for example, opening of the aminoterminal four-helix bundle in ApoE upon lipid binding is associated with enhanced receptor-binding activity. 65,66 HSA, the main protein present in plasma, has a good binding capacity for many substances, including ions, drugs, exogenous proteins, 67,68 and can function as a stabilizer. Since the magnetosome membrane contains lipids as well as proteins, we propose that during incubation, protein binding may be mediated by intrinsic membrane proteins through protein-protein interactions or by the interaction with membrane lipids that will induce conformational changes in the binding proteins.…”

Section: Discussionmentioning

confidence: 99%

<p>A Protein Corona Adsorbed to a Bacterial Magnetosome Affects Its Cellular Uptake</p>

Lai¹,

Li²,

Wang

et al. 2020

IJN

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It is well known that when exposed to human blood plasma, nanoparticles are predominantly coated by a layer of proteins, forming a corona that will mediate the subsequent cell interactions. Magnetosomes are protein-rich membrane nanoparticles which are synthesized by magnetic bacteria; these have gained a lot of attention owing to their unique magnetic and biochemical characteristics. Nevertheless, whether bacterial magnetosomes have a corona after interacting with the plasma, and how such a corona affects nanoparticle-cell interactions is yet to be elucidated. The aim of this study was to characterize corona formation around a bacterial magnetosome and to assess the functional consequences. Methods: Magnetosomes were isolated from the magnetotactic bacteria, M. gryphiswaldense (MSR-1). Size, morphology, and zeta potential were measured by transmission electron microscopy and dynamic light scattering. A quantitative characterization of plasma corona proteins was performed using LC-MS/MS. Protein absorption was further examined by circular dichroism and the effect of the corona on cellular uptake was investigated by microscopy and spectroscopy. Results: Various serum proteins were found to be selectively adsorbed on the surface of the bacterial magnetosomes following plasma exposure, forming a corona. Compared to the pristine magnetosomes, the acquired corona promoted efficient cellular uptake by human vascular endothelial cells. Using a protein-interaction prediction method, we identified cell surface receptors that could potentially associate with abundant corona components. Of these, one abundant corona protein, ApoE, may be responsible for internalization of the magnetosome-corona complex through LDL receptor-mediated internalization. Conclusion: Our findings provide clues as to the physiological response to magnetosomes and also reveal the corona composition of this membrane-coated nanomaterial after exposure to blood plasma.

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Section: Discussionmentioning

confidence: 99%

<p>A Protein Corona Adsorbed to a Bacterial Magnetosome Affects Its Cellular Uptake</p>

Lai¹,

Li²,

Wang

et al. 2020

IJN

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“…Other studies investigating hemolysin activity within the host revealed that oligomerization of toxin monomers inhibits toxin activity and this oligomerization can be enhanced by the addition of exogenous cholesterol (20,58,122,139,140). Conversely, the presence of membrane-bound cholesterol increased toxin binding to the erythrocyte membrane and was shown to be required for activity of the toxin (167,169).…”

Section: Cellular Damage and Cytotoxicitymentioning

confidence: 99%

“…These results suggest that cholesterol possesses a hemolysin receptor and, depending on the state of cholesterol (i.e., bound versus free), allows for either increased or decreased toxin activity. In addition to bound cholesterol, hemolysin monomers can also be stabilized by human serum albumin, thereby delaying oligomerization and its associated toxin inactivation (20). Studies examining the effect of cholesterol on hemolysin led to research into the effects of low-density lipoprotein (LDL) cholesterol on V. vulnificus lethality in diseased mice.…”

Section: Cellular Damage and Cytotoxicitymentioning

confidence: 99%

Vibrio vulnificus: Disease and Pathogenesis

2009

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Vibrio vulnificus is an opportunistic human pathogen that is highly lethal and is responsible for the overwhelming majority of reported seafood-related deaths in the United States (30,117). This bacterium is a part of the natural flora of coastal marine environments worldwide and has been isolated from water, sediments, and a variety of seafood, including shrimp, fish, oysters, and clams (4,7,25,26,43,97,109,116,118,149,165). Consumption of seafood (primarily raw oysters) containing V. vulnificus can result in a severe, fulminant systemic infection. Characteristics of this disease include fever, chills, nausea, hypotensive septic shock, and the formation of secondary lesions on the extremities of patients (11,22,41,74,115,146). This primary septicemia is the most lethal infection caused by V. vulnificus, with an average mortality rate exceeding 50% (30, 41). A review of 459 U.S. cases reported by the FDA between 1992 and 2007 (J. D. Oliver, unpublished) revealed that 51.6% of the patients died. Interestingly, 85.6% of the cases were male; this aspect of the infection is discussed later in this review. Of 180 cases in 2002 to 2007 for which FDA data were available, 92.8% of patients had consumed raw oysters prior to the onset of symptoms and 95.3% had some preexisting disease(s). The latter are clearly associated with V. vulnificus infection, with liver diseases, such as cirrhosis or hepatitis, being the most common (116). In addition to septicemia, V. vulnificus can produce serious wound infections that typically result from exposure of open wounds to water harboring the bacterium (114). Wound infections are frequently contracted as a result of recreational swimming, fishing injuries, or seafood handling (7, 46). Like systemic disease, wound infections progress rapidly to cellulitis, ecchymoses, and bullae, which can progress to necrotizing fasciitis at the site of infection; however, the mortality rate for wound infections (ca. 25%) is lower than that for systemic disease (10,13,74). This organism possesses a wide array of virulence factors, including acid neutralization, capsular polysaccharide expression, iron acquisition, cytotoxicity, motility, and expression of proteins involved in attachment and adhesion. These factors likely require concerted expression for pathogenesis to take place and appear to be under the control of global regulators. Overall, V. vulnificus is a complex microorganism with physiological characteristics that contribute to its survival in the marine environment and in the human host.

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“…Although albumin affects the activity of many different bacterial toxins, Choi et al reported that neither human serum albumin (HAS) nor bovine serum albumin (BSA) affected vvhA transcription or the growth of V. vulnificus. However, both HSA and BSA stabilized VVH and delayed its inactivation by oligomerization, thus enhancing VVH activity (42). Blood lipoproteins have also been shown to be an important defense factor against bacterial infection.…”

Section: Effects Of the Vvh On Eukaryotic Cellsmentioning

confidence: 99%

“…Meanwhile, a repressive interaction of H-NS would be relieved in response to the increase in temperature (39,49). LuxO is a central response regulator of the QS circuit in V. vulnificus, which negatively regulates vvhA expression via SmcR and HlyU (42,43). However, the transmembrane transcriptional activator ToxRS positively regulates the expression of the vvhA (47).…”

Section: Regulation Of Vvh Gene (Vvha) Expressionmentioning

confidence: 99%

Vibrio vulnificus Hemolysin: Biological Activity, Regulation of vvhA Expression, and Role in Pathogenesis

2020

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The Vibrio vulnificus (V. vulnificus) hemolysin (VVH) is a pore-forming cholesteroldependent cytolysin (CDC). Although there has been some debate surrounding the in vivo virulence effects of the VVH, it is becoming increasingly clear that it drives different cellular outcomes and is involved in the pathogenesis of V. vulnificus. This minireview outlines recent advances in our understanding of the regulation of vvhA gene expression, the biological activity of the VVH and its role in pathogenesis. An in-depth examination of the role of the VVH in V. vulnificus pathogenesis will help reveal the potential targets for therapeutic and preventive interventions to treat fatal V. vulnificus septicemia in humans. Future directions in VVH research will also be discussed.

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Human Serum Albumin Enhances the Hemolytic Activity of Vibrio vulnificus

Cited by 7 publications

References 24 publications

<p>A Protein Corona Adsorbed to a Bacterial Magnetosome Affects Its Cellular Uptake</p>

<p>A Protein Corona Adsorbed to a Bacterial Magnetosome Affects Its Cellular Uptake</p>

Vibrio vulnificus: Disease and Pathogenesis

Vibrio vulnificus Hemolysin: Biological Activity, Regulation of vvhA Expression, and Role in Pathogenesis

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