Neutrophil antimicrobial proteins enhance Shigella flexneri adhesion and invasion.
Cell Microbiol. 2010 Aug; 12(8):1134-43
This article PDF usually requires a subscription to access but you can receive the PDF, at no cost, through a special arrangement between Springer Science+Business Media and Faculty of 1000 for our Faculty Members who act as reviewers. This PDF is provided to you only for the purposes of reviewing the article while you consider preparing a recommendation of the article for F1000Prime. Other than for this purpose you warrant that you will treat the PDF as confidential. Furthermore you warrant that you will not use the PDF for any other purpose, especially but not limited to forwarding, copying, selling, distributing it whether commercially or non-commercially and that you will not make it available on any website for any other purpose.
This paper surprisingly shows that sublethal concentrations of antimicrobial proteins (AMPs) released by neutrophils can actually promote Shigella flexneri adhesion to and invasion into epithelial cells. This finding suggests a novel way for how this bacterium usurps weapons produced by the host to promote its own survival.
Neutrophils are generally able to kill bacteria using mechanisms including neutrophil extracellular traps (NETs), phagocytosis, and degranulation. As anticipated, increasing concentrations of an extract of purified human neutrophils in the presence of S. flexneri resulted in decreased bacterial viability in this study. However, in the presence of sublethal concentrations of this extract, similar to those encountered during the early stages of infection, there was actually an increase in bacterial adherence to epithelial cells. By using purified components, it was revealed that bactericidal permeability increasing protein (BPI) was responsible for this increased adherence and subsequent invasion. Interestingly, another serum protein that has a similar sequence and secondary structure, LPS-binding protein (LBP), did not show this effect. One of the differences between BPI and LBP is the charge of these molecules, suggesting that an electrostatic interaction with the surface of the bacteria may in part be responsible for these observations. It is very interesting that LL-37, another cationic antimicrobial, showed no effects on adhesion or invasion alone but could act synergistically with BPI. The authors hypothesize that this could be due to the different binding sites of the two proteins on bacterial LPS; however, this remains to be investigated. Although neutrophils are required for bacterial clearance, the findings reported here suggest that low levels of charged AMPs that are present early in infection may aid S. flexneri in altering its surface charge and escaping into epithelial cells, where it can multiply and spread. Further investigation into the specific interactions that allow this change in electrostatic charge could provide valuable insight into the molecular aspects of early Shigella infection. By understanding these interactions, it may be possible to modulate the surface charge to enhance host-protective mechanisms. While AMPs are not exploited in this manner by all invasive enteric bacteria, the surface charge interactions between the pathogen and host are likely critical for all encounters.
Goldberg J: F1000Prime Recommendation of [Eilers B et al., Cell Microbiol 2010, 12(8):1134-43]. In F1000Prime, 10 Aug 2010; DOI: 10.3410/f.4547975.4410079. F1000Prime.com/4547975#eval4410079
F1000Prime Recommendations, Dissents and Comments for [Eilers B et al., Cell Microbiol 2010, 12(8):1134-43]. In F1000Prime, 22 Aug 2014; F1000Prime.com/4547975
Get the most out of F1000Prime - attend a live online demonstration.
Please choose one of the following time zones:
Want to become an
has been added to your "Faculty I'm Following" page in MyF1000
Follow/Unfollow any Faculty via their recommendations, biography pages, or MyF1000
If you've forgotten your password, please enter your email address below and we'll send you instructions on how to reset your password.
The email address should be the one you originally registered with F1000.
You registered with F1000 via Google, so we cannot reset your password.
To sign in, please click here.
If you still need help with your Google account password, please click here.
You registered with F1000 via Facebook, so we cannot reset your password.
To sign in, please click here.
If you still need help with your Facebook account password, please click here.
We have sent an email to , please follow the instructions to reset your password.
If you don't receive this email, please check your spam filters and/or contact email@example.com.