Extracellular fibrinogen-binding protein (Efb), a key immune evasion protein of Staphylococcus aureus and a potential therapeutic target

نویسندگان

چکیده

Due to the continued growth of antibiotic-resistant Staphylococcus aureus strains, it is necessary explore alternative targets for future therapeutic applications. For this reason, important understand staphylococcal immune evasion mechanisms with a special focus on extracellular fibrinogen-binding protein (Efb) and Efb related proteins. Therefore, was conducted literature review compile relevant information protein. It found that has three binding sites biological relevance could be used as specificity fibrinogen, platelets, complements. First, motifs also in coagulase block neutrophil αMβ2 adherence fibrinogen attract bacterial surface, forming capsule-like structures phagocytosis. Second, potent anti-thrombotic agent, probably its P-selectin capacity. blocks interaction PSGL-1 receptor, thereby impairs platelet-mediated leukocyte recruitment site vascular injury. Third, complement domain, other inhibitory proteins like Ecb, Sbi, SCIN, responsible complement-mediated response. reduces formation C3 convertase neutrophils, affect B-cells activation, maturation. have clear implication virulence mastitis, wound infection, pneumonia, infections implanted devices, contributes persistence host tissues abscess kidneys. Given infections, they are promising vaccine targets. Additionally, due effect platelets complements, can potential agent treat diseases associated thrombosis abnormal activity.

برای دانلود باید عضویت طلایی داشته باشید

برای دانلود متن کامل این مقاله و بیش از 32 میلیون مقاله دیگر ابتدا ثبت نام کنید

اگر عضو سایت هستید لطفا وارد حساب کاربری خود شوید

منابع مشابه

Biological effects of Extracellular fibrinogen binding protein (Efb) in Staphylococcus aureus infection

Staphylococcus aureus is a leading cause of human and animal infection. The increasing incidence of antibiotic resistance among strains has complicated treatment of these infections. In order to develop new treatment strategies, it is important to identify and characterise bacterial factors that contribute to infection. S. aureus produces a diverse array of virulence factors, among these Extrac...

متن کامل

Extracellular Fibrinogen-binding Protein (Efb) from Staphylococcus aureus Inhibits the Formation of Platelet-Leukocyte Complexes*

Extracellular fibrinogen-binding protein (Efb) from Staphylococcus aureus inhibits platelet activation, although its mechanism of action has not been established. In this study, we discovered that the N-terminal region of Efb (Efb-N) promotes platelet binding of fibrinogen and that Efb-N binding to platelets proceeds via two independent mechanisms: fibrinogen-mediated and fibrinogen-independent...

متن کامل

Identification and characterization of the C3 binding domain of the Staphylococcus aureus extracellular fibrinogen-binding protein (Efb).

The secreted Staphylococcus aureus extracellular fibrinogen-binding protein (Efb) is a virulence factor that binds to both the complement component C3b and fibrinogen. Our laboratory previously reported that by binding to C3b, Efb inhibited complement activation and blocked opsonophagocytosis. We have now located the Efb binding domain in C3b to the C3d fragment and determined a disassociation ...

متن کامل

The extracellular fibrinogen-binding protein (Efb) from S

Staphylococcus aureus is an important human and animal pathogen that causes a wide range of infections. These infections can be very serious and sometimes hard to get rid of, because of the many virulence factors the bacteria produce during infections. This project was a research of the extracellular fibrinogen-binding protein, Efb, which is a 15.9 kDa protein that has been shown to be an impor...

متن کامل

Efb blocks interaction between P-selectin and PSGL-1 1 Extracellular Fibrinogen Binding Protein (Efb) from Staphylococcus aureus Inhibits the Formation of Platelet–Leukocyte Complexes

Extracellular fibrinogen binding protein (Efb) from Staphylococcus aureus inhibits platelet activation, although its mechanism of action has not been established. In this study we discovered that the N-terminal region of Efb (Efb-N) promotes platelet binding of fibrinogen and that Efb-N binding to platelets proceeds via two independent mechanisms: fibrinogen-mediated and fibrinogen-independent....

متن کامل

ذخیره در منابع من


  با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید

ژورنال

عنوان ژورنال: Current bioscience

سال: 2022

ISSN: ['2660-972X']

DOI: https://doi.org/10.51959/cb.2022.v2n1.e01