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Structure of antibody

Antibodies | Free Full-Text | IgG Antibody 3D Structures

Antibody Structure and Function Sino Biologica

All antibodies share struc- tural features, bind to antigen, and participate in a limited IgM, the First Responder number of effector functions. The antibodies produced in response to a particular anti- gen are heterogeneous General Structure of Antibodies Although there are different classes of antibodies, that is discussed further on in the article, the general structure of all antibodies is the same. They are fundamentally heavy globular proteins found in the plasma. The antibody molecule is made of four polypeptide chains - two heavy chains and two light chains

Antibody Structure - an overview ScienceDirect Topic

antibody structure The four-chain structure of an antibody, or immunoglobulin, molecule. The basic unit is composed of two identical light (L) chains and two identical heavy (H) chains, which are held together by disulfide bonds to form a flexible Y shape Antibodies are immune system-related proteins called immunoglobulins. Each antibody consists of four polypeptides- two heavy chains and two light chains joined to form a Y shaped molecule. The amino acid sequence in the tips of the Y varies greatly among different antibodies An antibody (Ab), also known as an immunoglobulin (Ig), is a large, Y-shaped protein used by the immune system to identify and neutralize foreign objects such as pathogenic bacteria and viruses.The antibody recognizes a unique molecule of the pathogen, called an antigen. Each tip of the Y of an antibody contains a paratope (analogous to a lock) that is specific for one particular epitope. The antibody base is known as the constant domain or constant region. The portion of an antigen that is recognized by the antibody is known as the epitope. Antibodies: (a) As a germ-line B cell matures, an enzyme called DNA recombinase randomly excises V and J segments from the light chain gene Structure of Antibody The structure of antibody was discovered by Rodney.R.porter and Gerald Edelman in 1962. All antibodies have a common basic structure. Each antibody molecule has 4 polypeptide chains. Two small called light chain(L) and two longer called heavy chain(H)

Antibody: Structure, classes and functions - Online

  1. Structure . An antibody or immunoglobulin (Ig) is a Y-shaped molecule. It consists of two short polypeptide chains called light chains and two longer polypeptide chains called heavy chains. The two light chains are identical to each other and the two heavy chains are identical. At the ends of both the heavy and light chains, in the areas that.
  2. An antibody is Y-shaped and is composed of four polypeptides, two heavy chains, and two light chains, identical, joined together by disulfide bonds. There are five types of the heavy chains, termed gamma (γ), mu (μ), alpha (α), delta (δ), and epsilon (ε), and two types of light chains, lambda (λ) and kappa (κ)5
  3. Antibody molecules have a highly specialized structure that can mediate biological response upon specifically binding to an antigen. This chapter introduces readers to the chemical structure of antibodies, with specific focus on the structure of immunoglobulin G (IgG)
  4. Structure of Antibodies. The antibody recognizes a unique part of an antigen (foreign object). Each tip of the Y of an antibody contains a paratope (a structure analogous to a lock) that is specific for one particular epitope (similarly analogous to a key) on an antigen, allowing these two structures to bind together with precision
  5. o acid residues. The structure of mAbs is far more complex than small molecule drugs, including the primary structure, higher order structure, charge variants, and glycosylation variants, etc. Changes to mAb structure.
  6. The first atomic resolution structure of an antibody fragment was published in 1973 (12) and this was quickly followed by the invention of monoclonal antibodies in 1975 by Georges Köhler and César Milstein (13) signalling the start of the modern era of antibody research and discovery. << Antibody overview Antibody structure >>
  7. Antibody Structure and Function 1. J O A N N A I S M Y N A M E CHAPTER 4 ANTIBODY STRUCTURE AND FUNCTION 2. IMMUNOGLOBULINS • are glycoproteins found in the serum portion of the blood • Composed of 82% - 96% polypeptide and 2% - 14% carbohydrate • Humoral branch of the immune response • Primary role is antigen recognition and in biological activities related to immune response and.

This antibody tutorial explains the structure of antibody and immunoglobin molecules. For more information, log on to- http://shomusbiology.weebly.com/ Downl.. On the surface of the complex structure of the antibody is a spot on the tips of each of its floppy, Y-shaped arms. This infinitesimally small patch of molecules can neatly stretch across a spot on the coronavirus spike, a site that otherwise works like a grappling hook to grab onto a docking site on human cells The function of an antibody binding to an antigen is provided by the structure of the variable region which has the antigen-binding site (known as the Fragment antigen-binding fragment made from one constant and one variable region); the variable amino acid configuration allows a diverse possibility of specific antibodies to bind with antigens. Polyclonal antibodies, which are generally purified directly from serum, are especially useful as labeled secondary antibodies in immunoassays. Because an individual B-lymphocyte produces and secretes only one specific antibody molecule, clones of B-lymphocytes produce monoclonal antibodies Structure-based development of human antibody cocktails against SARS-CoV-2. Structure-based development of human antibody cocktails against SARS-CoV-2 Cell Res. 2020 Dec 1;1-3. doi: 10.1038/s41422-020-00446-w. Online ahead of print. Authors Nan Wang 1.

Antibodies | Free Full-Text | Antibody Aggregation

Antibody : Types, Structure, Classes and Functions

Structure of antibodies. The variable region and the constant region . The N-terminal domains of the H and L chains are called the variable regions (V regions), and the rest of the molecule is called the constant region (C region). The amino acid sequence of the V region varies from antibody to antibody, accounting for the high degree of three. Get a quick overview of Structure of the Antibody from Antibodies - Structure and Function (Advanced) and Antibody - Structure and Function and Antigens and Antibodies and Immunoglobulins and Acquired Immunity and Antibodies (Intermediate) in just 3 minutes

Structure of antibody molecule Topic: Immune System. An antibody is formed of four polypeptide chains: two heavy and two light chains bound in a Y shape. An antibody is a molecule that recognizes a specific antigen; this recognition is a vital component of the adaptive immune response. Antibodies are composed of four polypeptides: two identical. The very basic structure of an immunoglobulin (antibody) molecule can be demonstrated under following points: Polypeptide chains: Antibody molecules have a common struc­ture of four polypeptide chains, having two different sizes. These are a pair of identical high molecular weight chains called Heavy chains (H-chains) and a pair of identical.

Draw the stick figure structure of IgG, indicating the Fab portion (variable region) and the Fc portion (constant region). State the functions of the Fab and the Fc portions of an antibody. State what is meant by the biological activity of an antibody. Compare the structure of IgM and secretory IgA with that of IgG Antibodies represent the quintessential effector molecules of the adaptive immune system. They display tremendous variation in structure, allowing the immune system to quickly adapt to invading pathogens, recognizing a virtually unlimited number of structures, and combining this with a large variety of functional traits in a modular fashion Presentation antibody and structure 1. ANTIBODIES Sajid Khan ROLL NO. :- BC582125 M.Sc MICROBIOLOGY 3rd Semester, Allama iqbal open university Islamabad 2. DEFINITION: An antibody or immunoglobulin (Ig) is a glycoprotein that is made by plasma cells in response to an antigen and can recognize and bind to the antigen that caused its production. 3 The basic structure, however, remains the same: 4 antibody chains are held together by a combination of non-covalent interactions and covalent bonds (disulfide linkages) in such a way that they form a Y-shaped molecule. The 2 antigen binding sites are at the a-terminus of the light and heavy chains at the ends of the arms of the Y

Antibodies and antibody-derived macromolecules have established themselves as the mainstay in protein-based therapeutic molecules (biologics). Our knowledge of the structure-function. Antibodies—Structure and Sequence: This Web site summa- c. All immunoglobulin molecules on the surface of a given rizes useful information on antibody structure and sequence. B cell have the same isotype. It provides general information on antibodies and crystal d Antibody Structure and Classes. History of Immunoglobulin Molecules. Take a look at our Timeline - History of Immunoglobulin Molecules. History of Immunoglobulin Molecules. Immunoglobulin Structure. The immunoglobulins are a family of glycoproteins, and based on chemical and structural differences are classified in five distinct classes of. The structure of one class of antibody: Structure of antibodies Antibodies are Y-shaped glycoprotein molecules (Figures 3 and 4). Glycoproteins are proteins with carbohydrate attached. Each antibody molecule has four polypeptide chains, comprising two identical pairs of light and heavy chains. Disulphide bridges hold the assembly together Instead, people sequence the DNA corresponding to a given antibody instead of sequencing the antibody protein itself. As a given B cell expresses one antibody in large amounts, Milstein and Kohler (Nobel laureates) devised a technique to fuse B cells with tumor cells, creating hybridomas. Each hybridoma thus produces a single antibody

Antibody- Introduction, Structure and Classe

  1. al domain is the most.
  2. Structural studies on antibody recognition of HIV Env have revealed that these broadly reactive antibodies target epitopes covering entire exposed and glycosylated surface on the viral spike; several classes of antibodies recognize the viral spike with converged modes. Critical structural features, such as antibody mimicry of cellular receptors.
  3. Antibody Structure. An antibody is a molecule that recognizes a specific antigen; this recognition is a vital component of the adaptive immune response. Antibodies are composed of four polypeptides: two identical heavy chains (large peptide units) that are partially bound to each other in a Y formation, which are flanked by two identical.
  4. Antibodies are glycoproteins which are highly specific to antigens. They are also known as immunoglobulins (Igs). They have a 'Y' shaped structure. It consists of four polypeptide chains, two heavy (H) chains and two light (L) chains. The four polypeptide chains are held together by disulfide bonds to form a 'Y' shaped structure
  5. To learn more about how antibodies operate, review the accompanying lesson on The Structure of Antibodies. This lesson covers the following objectives: Understanding the four chains of protein.

Antibody Structure Absolute Antibody

Thus, IgM antibodies are very efficient in leading to the lysis of microorganisms. As a consequence of its structure, IgM is also a good agglutinating Ig . Thus, IgM antibodies are very good in clumping microorganisms for eventual elimination from the body. IgM binds to some cells via Fc receptors Antibodies are gammaglobulin proteins, predominantly referred to as immunoglobulins (Ig). A monomeric antibody is composed of two heavy chains and two light chains covalently linked together through disulfide bonds to generate a Y-shaped structure (Figure 1) The first atomic resolution structure of an antibody fragment was published in 1973 (12) and this was quickly followed by the invention of monoclonal antibodies in 1975 by Georges Köhler and César Milstein (13) signalling the start of the modern era of antibody research and discovery Illustration about Three-dimensional structure of an antibody molecule. Illustration of disease, computational, molecule - 39587 Immunoglobulin G4 antibodies exhibit unusual properties with important biological consequences. We report the structure of the human full-length IgG4 S228P anti-PD1 antibody pembrolizumab, solved to 2.3-Å resolution. Pembrolizumab is a compact molecule, consistent with the presence of a short hinge region

All catalytic antibodies, whose crystal structure had been solved until now, belonged to the 95% mouse antibodies that possess a κ-light chain , except one . Many of these catalytic antibodies share a deep combining site formed not only by residues of the CDRs but also by residues of the framework ( Figure 8C ) [58] , [61] Anti-Fab antibodies bound to both heavy and light chains; Anti-Fc antibodies bound only to heavy chains. These data lead to proposal of a Y-shaped structure by Porter in 1962, many years before the 1 st crystal structure was known. Structure and Function of IgG: Prototypical Antibody Structure: Quaternary Structure Antibody Structure. Antibodies are composed of four chains, two long heavy chains (colored red and orange) and two shorter light chains (yellow). The specific binding site is found at the tips of the two arms, in a pocket formed between the light and heavy chain. The binding site is composed of several loops in the protein chain that have very. Madej T, Lanczycki CJ, Zhang D, Thiessen PA, Geer RC, Marchler-Bauer A, Bryant SH. MMDB and VAST+: tracking structural similarities between macromolecular complexes. Nucleic Acids Res. 2014 Jan; 42(Database issue):D297-303:D297-30 Scientists at Fred Hutchinson Cancer Research Center in Seattle have shown that a potent antibody from a COVID-19 survivor interferes with a key feature on the surface of the coronavirus' distinctive spikes and induces critical pieces of those spikes to break off in the process.. The antibody—a tiny, Y-shaped protein that is one of the body's premier weapons against pathogens including.

The antibodies identified here may be candidates for development of clinical interventions against SARS-CoV-2. Organizational Affiliation : Center for Global Health and Infectious Diseases, Comprehensive AIDS Research Center and Beijing Advanced Innovation Center for Structural Biology, School of Medicine, and Vanke School of Public Health. Lv et al. report a humanized monoclonal antibody that protected against SARS-CoV-2 in a mouse model. The cryo-electron microscopy structure, together with biochemical, cellular, and virological studies, showed that the antibody acts by binding to the receptor-binding domain of the spike and blocking its attachment to the host receptor Thus, antibody H3 modeling is the most important and difficult step of antibody structure modeling. Loop Modelling . The first problem is a group of missing residues in an antibody structure, where the sequence of the missing segment is known, whereas the three-dimensional structure of those residues is not The RBD-B38 complex structure revealed that most residues on the epitope overlap with the RBD-ACE2 binding interface, explaining the blocking effect and neutralizing capacity. Our results highlight the promise of antibody-based therapeutics and provide a structural basis for rational vaccine design

(PDF) Antibody Structure & Function magendira mani

  1. ant) antigens have many unique epitopes that multiple antibodies can bind to structure of antibody
  2. Discovering the Molecular Structure of Antibodies and Elaborating the Sciences of Recognition Antibodies are proteins made by the immune system. They seek out specific antigens-toxins, the cell walls of bacteria, or the outer coats of virus particles, for example-to disable these invaders or signal other cells to remove them
  3. e the structural basis of neutralization, we generated cryogenic electron microscopy reconstructions of Fab:CHIKV complexes at 4- to 5-Å resolution
  4. On the surface of the complex structure of the antibody is a spot on the tips of each of its floppy, Y-shaped arms. This infinitesimally small patch of molecules can neatly stretch across a spot.

Despite demonstrated protection by NS1-specific antibodies against lethal flavivirus challenge, the structural and mechanistic basis remains unknown. Here, we present three crystal structures of full-length dengue virus NS1 complexed with a flavivirus-cross-reactive, NS1-specific monoclonal antibody, 2B7, at resolutions between 2.89 and 3.96.

Types of Antibodies in Blood Properties, Structures

antibody Definition, Structure, Function, & Types

Human antibodies are classified into five isotypes (IgM, IgD, IgG, IgA, and IgE) according to their H chains, which provide each isotype with distinct characteristics and roles. IgG IgG is the most abundant antibody isotype in the blood (plasma), accounting for 70-75% of human immunoglobulins (antibodies) Determining antibody CDR cluster. For each PDB structure with an identified antibody VH or VL domain, we determine the CDR sequences and their lengths, which represents the first level of our classification system (e.g. L1-11, L2-8, etc.) Illustration about Three-dimensional structure of an antibody molecule. Illustration of immunity, disease, antigen - 38902 The basic structure of a conventional full size antibody (left panel) and of common antibody fragments (right panel). From [ 1 ] Each complete antibody has two antigen-binding pockets, located in the F V regions, and can bind to two antigens (bivalent binding) Antibody Structure An antibody is a molecule that recognizes a specific antigen; this recognition is a vital component of the adaptive immune response. Antibodies are composed of four polypeptides: two identical heavy chains (large peptide units) that are partially bound to each other in a Y formation, which are flanked by two identical.

Antibody is a part of the host cell's defense. It's made by a certain type of white blood cell that's called a B cell. The structure of the antibody consists of two light chains and two heavy chains, and at the very tip of the antibody is a hypervariable region, and this hypervariable region allows the antibody to make different types of antibodies that will respond to all of the antigens that. The κ and λ chains are found 67% and 33% of the time, respectively. Any antibody can be formed by the association of one heavy chain type with one light chain type. In every possible combination there will be two identical heavy and light chains in the antibody unit (monomer). Hence the IgM pentamer can either comprise (μ 2 κ 2) 5 or (μ 2. Structural diversity has been fast-growing in the bispecific antibody field, creating a plethora of novel bispecific antibody scaffolds, which provide great functional variety. Two common formats of bispecific antibodies on the market are the single-chain variable fragment (scFv)-based (no Fc fragment) antibody and the full-length IgG-like.

Antibody Structure - University of Arizon

Antibody Structure. Antibodies are glycoproteins.The basic functional unit of each antibody is an immunoglobulin (Ig) monomer (containing only one Ig unit); secreted antibodies can also be dimeric with two Ig units as with IgA, tetrameric with four Ig units like teleost fish IgM, or pentameric with five Ig units, like mammalian IgM.. Core structure of camelid antibodies. In conventional antibodies, the light chain is bound to the constant region, CH1. However, in camelid antibodies, a single N-terminal variable domain heavy. 2) They contain 2 light chains and 2 heavy chains allowing a sturdy structure, also allowing for 2 variable regions so multiple antigens can be attached. 3) The variable region is specific to an antibody hence allowing specificity to different antigens. 4) The antibody contains a constant region also called Fc which can bind to phagocyte Antibodies and antibody-derived macromolecules have established themselves as the mainstay in protein-based therapeutic molecules (biologics). Our knowledge of the structure-function relationships of antibodies provides a platform for protein engineering that has been exploited to generate a wide range of biologics for a host of therapeutic indications Antibody definition is - any of a large number of proteins of high molecular weight that are produced normally by specialized B cells after stimulation by an antigen and act specifically against the antigen in an immune response, that are produced abnormally by some cancer cells, and that typically consist of four subunits including two heavy chains and two light chains —called also.

Antibody - Wikipedi

  1. Same antibody: select the known structure that can provide a template for both the heavy and light chain, even if a different template with a higher sequence identity exists for one of the chains. If two different antibodies are selected for each chain, the program needs to reconstruct the complete molecule by matching residues known to be.
  2. ed a 3.4 Å single-particle cryo-EM structure of the complex of one such antibody (C105; IC 50 for neutralization of SARS-CoV-2 pseudovirus = 26.1 ng/mL) (Robbiani et al., 2020) bound to the SARS-CoV-2 S protein using a 1.8 Å crystal structure of the unbound C105 Fab for fitting to the cryo-EM density (Figures 5, S5, and S6; Tables.
  3. The human antibody repertoire is one of the most important defenses against infectious disease, and the development of vaccines has enabled the conferral of targeted protection to specific pathogens. However, there are many challenges to measuring and analyzing the immunoglobulin sequence repertoire, including that each B cell's genome encodes a distinct antibody sequence, that the antibody.
  4. Structure of an Antibody It is important to learn about the structure of an antibody and why they are such important molecules in immunocytochemistry
  5. Structure of an antibody molecule (IgG). Fab fragment (fragment antigen binding) is composed of a bonded whole light chain (with one V and one C region) and a heavy chain's V and first C region and recognizes the antigen. The Fc fragment (fragment crystalline) is the remaining region of heavy chain
  6. The structure of an antibody can be divided into an upper Fab fragment (antibody binding fragment) and a lower Fc fragment (crystallizable fragment). The Fab region binds to the antigen via the epitopes present on the antigen surface. The Fc region interacts with other immune cells and recruits them to mediate the clearance of the antigen

Antibodies Boundless Biolog

Antibody humanization—the Influence of the antibody framework on the CDR-H3 loop ensemble in solution. Protein Engineering, Design and Selection 2019 , 32 (9) , 411-422 These include antibodies, contractile proteins, enzymes, hormonal proteins, structural proteins, storage proteins, and transport proteins. Antibodies Their ability to travel through the bloodstream enables them to be utilized by the immune system to identify and defend against bacteria, viruses, and other foreign intruders in blood

Coronaviruses (CoVs) are enveloped positive-sense RNA viruses. The club-like spikes projecting out from their surface gave them the name. Coronaviruses possess an unusual large RNA genome as well as a unique replication strategy. Coronaviruses cause a variety of diseases in animals ranging from cows, pigs to chicken, and other birds. In humans, coronaviruses can cause potentially lethal. Antibody CAP256-VRC26.25 is one of the most potent known HIV-1-neutralizing antibodies. Gorman et al. determine the cryo-EM structure of this antibody in complex with the Env trimer that initiated the antibody lineage. The structure reveals how elements of distinct antibody classes can intermingle to yield an antibody of extraordinary potency Developing antibody agonists targeting the human apelin receptor (APJ) is a promising therapeutic approach for the treatment of chronic heart failure. Here, we report the structure-guided discovery of a single-domain antibody (sdAb) agonist JN241-9, based on the cocrystal structure of APJ with an sdAb antagonist JN241, the first cocrystal structure of a class A G protein-coupled receptor. However, variations in the structure of the loops alter this surface enough to allow different antibodies to recognize completely different molecules. In 2016, a new class of antibodies was identified. Unlike previously identified antibodies, these molecules had an entire human protein, called LAIR1, inserted into one of their CDR loops The structure of an intact, anti-canine lymphoma monoclonal antibody (Mab231) was determined by molecular replacement and refined in a triclinic cell to an R-value of 20.9%, using synchrotron.

Structure of the Antibody Molecule. Antibodies are glycoproteins produced by B lymphocytes in both membrane-bound and secreted forms. They are composed of two heavy chains and two light chains. In general, the two heavy chains are linked by disulfide bonds, and each heavy chain is linked to a light chain by a disulfide bond The 2019 coronavirus pandemic remains a major public health concern. Neutralizing antibodies (nAbs) represent a cutting-edge antiviral strategy. We focus here on severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) and SARS-CoV, and discuss current progress in antibody research against rampant SARS-CoV-2 infections. We provide a perspective on the mechanisms of SARS-CoV-2-derived nAbs. The structure of all* immunoglobulins consists of four chains: two identical light chains and two identical heavy chains make up the recognizable Y shape of the antibody. The chains are held together by inter-chain disulfide bonds and by non-covalent interactions which vary between the different immunoglobulin isotypes

In general, an antigen is defined as a substance that binds to specific antibodies, which in the human body are used to find and neutralize any potentially harmful foreign substances in the bloodstream. The specific binding between antigen and antibody is similar to that of the lock-and-key binding model The antibody specificity for any given antigen is underscored by its unique structure, which allows antigen binding with high precision. Because antibodies are highly specific, they serve as very useful tools in scientific research to elucidate the location, abundance, and function of proteins in dynamic biological systems d Explain how the structure of an antibody such as the antitoxin for choleragen from BS MISC at University of Nottingham Malaysia Campu

Structure of Antibody - SlideShar

Introduction The higher-order protein structure and protein dynamics basically determine the personality of a protein, 1,2 therefore, comprehensive characterization of these structure features is essential for a better understanding of their functions. This is of particular importance for the development of antibody drugs and biosimilars, as even a small change in their higher-order. Here we report the structure at 3.5 A resolution of an IgG2a antitumour monoclonal antibody which contains an intact hinge region and was solved in a triclinic crystal by molecular replacement using known Fc and Fab fragments. The antibody is asymmetric, reflecting its dynamic character. There are two local, apparently independent, dyads in the. Structural analysis of the NA-antibody fragment antigen-binding (Fab) complex provides a clue for antibody modification, and the modified antibody restored binding and inhibition to recently drifted N1 NA and regained protection against the variant influenza strain. This finding suggests that antibodies to NA may be a useful therapy and can be.

Structural insights for Fc interactions and the3D movie of Immunoglobulin G (IgG) molecule - YouTubeStructural Damage in Rheumatoid ArthritisToxins | Free Full-Text | Crystal Structure of theRoche - Monoclonal AntibodiesCancers | Free Full-Text | Role of Tertiary Lymphoid
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