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Micrograph shows a round cell with a large nucleus.
Lymphocytes, such as NK cells, are characterized by their large nuclei that actively absorb Wright stain and therefore appear dark colored under a microscope.

An infected cell (or a tumor cell) is usually incapable of synthesizing and displaying MHC I molecules appropriately. The metabolic resources of cells infected by some viruses produce proteins that interfere with MHC I processing and/or trafficking to the cell surface. The reduced MHC I on host cells varies from virus to virus and results from active inhibitors being produced by the viruses. This process can deplete host MHC I molecules on the cell surface, which NK cells detect as “unhealthy” or “abnormal” while searching for cellular MHC I molecules. Similarly, the dramatically altered gene expression of tumor cells leads to expression of extremely deformed or absent MHC I molecules that also signal “unhealthy” or “abnormal.”

NK cells are always active; an interaction with normal, intact MHC I molecules on a healthy cell disables the killing sequence, and the NK cell moves on. After the NK cell detects an infected or tumor cell, its cytoplasm secretes granules comprised of perforin    , a destructive protein that creates a pore in the target cell. Granzymes are released along with the perforin in the immunological synapse. A granzyme    is a protease that digests cellular proteins and induces the target cell to undergo programmed cell death, or apoptosis. Phagocytic cells then digest the cell debris left behind. NK cells are constantly patrolling the body and are an effective mechanism for controlling potential infections and preventing cancer progression.

Complement

An array of approximately 20 types of soluble proteins, called a complement system    , functions to destroy extracellular pathogens. Cells of the liver and macrophages synthesize complement proteins continuously; these proteins are abundant in the blood serum and are capable of responding immediately to infecting microorganisms. The complement system is so named because it is complementary to the antibody response of the adaptive immune system. Complement proteins bind to the surfaces of microorganisms and are particularly attracted to pathogens that are already bound by antibodies. Binding of complement proteins occurs in a specific and highly regulated sequence, with each successive protein being activated by cleavage and/or structural changes induced upon binding of the preceding protein(s). After the first few complement proteins bind, a cascade of sequential binding events follows in which the pathogen rapidly becomes coated in complement proteins.

Complement proteins perform several functions. The proteins serve as a marker to indicate the presence of a pathogen to phagocytic cells, such as macrophages and B cells, and enhance engulfment; this process is called opsonization    . Certain complement proteins can combine to form attack complexes that open pores in microbial cell membranes. These structures destroy pathogens by causing their contents to leak, as illustrated in [link] .

Illustration shows an invading pathogen with an antigen on its surface. In the classic pathway for complement activation, host antibodies bind the antigen, and C1 binds the antibody. The C1-antibody complex causes C2 and C4 each to split in two. Fragments from C2 and C4 each joins together to form an enzyme called C3 convertase. C3convertase splits C3 in two. One of the fragments from C3 joins C3 convertase to form C5 convertase. C5 convertase splits C5 in two. A fragment from C5 joins C6, C7, C8, and C9 to form a complex that makes a hole in the plasma membrane for the invading cell. The cell swells and bursts. In the alternative pathway, C3 convertase spontaneously splits C3 in two and the rest of the pathway proceeds the same as the classic pathway. Host cells are protected from complement by the presence of endogenous proteins.
The classic pathway for the complement cascade involves the attachment of several initial complement proteins to an antibody-bound pathogen followed by rapid activation and binding of many more complement proteins and the creation of destructive pores in the microbial cell envelope and cell wall. The alternate pathway does not involve antibody activation. Rather, C3 convertase spontaneously breaks down C3. Endogenous regulatory proteins prevent the complement complex from binding to host cells. Pathogens lacking these regulatory proteins are lysed. (credit: modification of work by NIH)

Section summary

The innate immune system serves as a first responder to pathogenic threats that bypass natural physical and chemical barriers of the body. Using a combination of cellular and molecular attacks, the innate immune system identifies the nature of a pathogen and responds with inflammation, phagocytosis, cytokine release, destruction by NK cells, and/or a complement system. When innate mechanisms are insufficient to clear an infection, the adaptive immune response is informed and mobilized.

Questions & Answers

explain the importance of carbon dioxide in the body
Kiiza Reply
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SAMUEL
diagram of Prokaryotic cells
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Yazi
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Sahfe Reply
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James
genotype: this is the combination of alleles an organism has for a given characteristic..
Cosmo
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Gabriel Reply
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Gabriel
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Harleen Reply
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Kags Reply
no
Bernard
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kf
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James
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Ronald Reply
tissue combined to form organ
zameer
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Elishs
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Elishs
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Kags
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Harleen
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Bernard
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zameer Reply
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Tariro Reply
biology is the study of living organisms
Bernard
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Nantamu
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zameer
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Jesus Reply
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Francis
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Francis
A cell is the basic functional unit of life.
Jael
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Rabecca Reply
A cell is the basic functional unit of all organisms
Glandwell
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Mavis
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Sabrinah
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Tamirat
renin,pepsin
Nyakato
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Nathan Reply
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zameer
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linus
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Onuoha
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mejury
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Toyyiba
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Nyakato
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Peace
What is Diffusion
Soliu
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adewunmi
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Peace
what is zameer
Francis

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Source:  OpenStax, Biology. OpenStax CNX. Feb 29, 2016 Download for free at http://cnx.org/content/col11448/1.10
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