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In S. aureus, cell-wall-anchored proteins and other adhesive molecules are implicated in binding to host matrix molecules and may therefore play an essential role in the establishment of colonization.
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Recently, Edwards and colleagues demonstrated that the central region of MSP mediates its binding to host extracellular matrix (ECM) components and that this area is the preferential target of host immune responses.
For example, the cell-wall-associated proteins SpsD and SpsL are expressed by S. pseudintermedius during canine infection, are immunogenic and mediate binding to host extracellular matrix proteins, suggesting a role in disease pathogenesis [ 13].
Hemagglutinin plays a major role in determining host specificity since it is responsible for viral binding to host cell receptors and penetration of host membranes [5], [6], [7].
There are some examples of PfEMP1 variants where binding to host receptors is localized to a single domain (for example, CIDRα binding CD36 [49] or DBLβC2 binding ICAM-1 [50].
Firstly, this analysis has to be applied to host matrix without embedded nanoparticles having (τ 1 host, I 1 host), (τ 2 host, I 2 host), and (τ 3 host, I 3 host) component inputs in three-term decomposed row PAL spectrum (I 1 host + I 2 host + I 3 host = 1).
These adhesins facilitate binding to various matrix proteins or host cells [29].
Staphylococcal adhesion to host cells is often mediated through binding to bridging matrix molecules, which are likewise bound by the host cells via specific receptors like β1-integrins [35].
They are able to contribute to microbial adhesion by binding to extracellular matrixes (ECMs) of host cells and initiate infection [1].
Included among the host of physiologic processes in diarthrodial joints regulated by these species are regulation of matrix metalloproteinases (MMPs), aggrecanase, plasmin, tissue mitogens and angiogenesis activity, as well as inhibition of inflammatory leukocyte proteases such as neutrophil elastase and regulation of fibroblast mitogen binding to extracellular matrix [ 32- 42].
This greatly reduced the binding of native E. coli proteins binding to the matrix.
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