Antiadenovirus activity of milk proteins: lactoferrin prevents viral infection

Arnold, Daria; Biase, Assunta Maria Di; Marchetti, Magda; Pietrantoni, Agostina; Valenti, Piera; Seganti, L; Superti, Fabiana

doi:10.1016/s0166-3542(01)00197-8

Cited by 81 publications

(52 citation statements)

References 31 publications

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“…Thus, HLf promoted infection by Ad5 in cells that corresponded to the normal tropism of this virus. From previous work by others, it has been suggested that HLf inhibits Ad2 from infecting Hep2 cells (3,13). In these studies, however, the concentrations of HLf that were inhibitory (0.5 mg/ml abolished 50% of the cytopathic effect) were higher than those we found to promote Ad5 infection in HCE, A549, and Hep2 cells.…”

Section: Tear Fluid Promotes Ad5 Infection Of Corneal Cellscontrasting

confidence: 72%

“…One possible explanation for this is that at very high concentrations, individual HLf proteins bind to either virions or cells, but not to both, and thus HLf may be prevented from forming the bridge that is required for linking virions to cells, giving results similar to those described previously (3,13). Assuming 2 mg/ml HLf in tear fluid (51), the dilution used here (1:10) corresponds to 0.2 mg/ml, which is within the range in which HLf was found to act as a promoter of virus binding.…”

Section: Tear Fluid Promotes Ad5 Infection Of Corneal Cellssupporting

confidence: 72%

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Adenoviruses Use Lactoferrin as a Bridge for CAR-Independent Binding to and Infection of Epithelial Cells

Johansson¹,

Jönsson²,

Marttila³

et al. 2007

J Virol

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Most adenoviruses bind to the coxsackie-and adenovirus receptor (CAR). Surprisingly, CAR is not expressed apically on polarized cells and is thus not easily available to viruses. Consequently, alternative mechanisms for entry of coxsackievirus and adenovirus into cells have been suggested. We have found that tear fluid promotes adenovirus infection, and we have identified human lactoferrin (HLf) as the tear fluid component responsible for this effect. HLf alone was found to promote binding of adenovirus to epithelial cells in a dose-dependent manner and also infection of epithelial cells by adenovirus. HLf was also found to promote gene delivery from an adenovirus-based vector. The mechanism takes place at the binding stage and functions independently of CAR. Thus, we have identified a novel binding mechanism whereby adenovirus hijacks HLf, a component of the innate immune system, and uses it as a bridge for attachment to host cells.

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Section: Tear Fluid Promotes Ad5 Infection Of Corneal Cellscontrasting

confidence: 72%

Section: Tear Fluid Promotes Ad5 Infection Of Corneal Cellssupporting

confidence: 72%

Adenoviruses Use Lactoferrin as a Bridge for CAR-Independent Binding to and Infection of Epithelial Cells

Johansson¹,

Jönsson²,

Marttila³

et al. 2007

J Virol

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“…Hence, an ideal microbicide should also have a broad spectrum of activity against a variety of sexually transmitted microbes within genital secretions (58,59). And it's the case of Lf, which is active against a large spectrum of bacteria (60), parasites (61), and viruses such as herpes simplex virus type 1 and 2 (28), adenovirus (62), HIV (63)(64)(65), hepatitis B (66) and C (67) virus, human CMV (63,68), hantavirus (69), retrovirus 71 (70), and alphavirus (16).…”

Section: Discussionmentioning

confidence: 99%

Differential Modulation of Human Lactoferrin Activity against Both R5 and X4-HIV-1 Adsorption on Epithelial Cells and Dendritic Cells by Natural Antibodies

Saïdi

Eslaphazir

Carbonneil

et al. 2006

The Journal of Immunology

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Human lactoferrin (Lf) is an iron binding glycoprotein that is present in several mucosal secretions. Many biological functions have been ascribed to Lf. In the present study, we showed that Lf limited specifically adsorption of R5- and X4-HIV-1-free particles on endometrial epithelial HEC-1A cells, by inhibiting virus adsorption on heparan-sulfated proteoglycans. But, Lf did not interfere with both R5 and X4-HIV transcytosis. We showed also the efficacy of Lf in preventing R5 and X4-HIV capture by dendritic cells. Conversely, we demonstrated that Lf-reacting natural Abs (NAbs) present within i.v. Ig-enhanced HIV attachment on dendritic cells by forming HIV-Lf-NAbs. HIV particles were able to directly interact with Lf following its interaction with NAbs. We also found Lf-reacting natural Abs within cervicovaginal secretions, suggesting the existence of Lf-NAbs complexes in women genital tract in vivo. In conclusion, this study highlights Lf as a potent microbicides and reports new function for NAbs within the genital compartment that may compartment that may abolish the inhibitory activity of microbicide compounds. Thus, we proposed a model in which Lf would appear as a double-edged sword that could have beneficial or detrimental effects depending on both cellular and molecular environments. This study highlights the use of Lf derivates as microbicide candidates to limit such interferences.

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“…Human lactoferrin (apo-or Fe 3+ ), -lactalbumin, -lactoglobulin, human lactadherin, mucin, and immunoglobulin from milk could prevent rotavirus infection through the binding to structural viral protein VP4 [30,37,38,40,107,108]. Also, the antiviral activity of lactoferrin against adenovirus has been attributed to the interaction of the milk protein with viral capsid proteins [60,61,69].…”

Section: Binding To Structural Virus Proteins Prevent Virus Host Cellmentioning

confidence: 99%

Milk Derived Peptides with Immune Stimulating Antiviral Properties

Sun¹,

Jenssen²

2012

Milk Protein

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Antiadenovirus activity of milk proteins: lactoferrin prevents viral infection

Cited by 81 publications

References 31 publications

Adenoviruses Use Lactoferrin as a Bridge for CAR-Independent Binding to and Infection of Epithelial Cells

Adenoviruses Use Lactoferrin as a Bridge for CAR-Independent Binding to and Infection of Epithelial Cells

Differential Modulation of Human Lactoferrin Activity against Both R5 and X4-HIV-1 Adsorption on Epithelial Cells and Dendritic Cells by Natural Antibodies

Milk Derived Peptides with Immune Stimulating Antiviral Properties

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