**14. Conclusion**

Biochemical and molecular studies of numerous lectins eventually demonstrated that only a limited number of carbohydrate-binding motifs evolved in plants (Peumans et al. 2000). Since the specificity of these binding motifs is primarily directed against foreign glycans, it is generally accepted now that many plant lectins are involved in the recognition and binding of glycans from foreign organisms, and accordingly play a role in plant defense (Peumans and Van Damme 1995; and Van Damme et al. 1998). Most plant lectins are probably involved in the plant's defense. Whereas direct interference with viruses and microorganisms are rather exceptional, the deleterious effects of plant lectins on predatory invertebrates and higher animals are obvious. Considering the abundance of lectins in storage organs and their storage protein-like behavior, we believe that plants accumulate part of their nitrogen reserve in the form of carbohydrate-binding proteins, which can be used as passive-defense proteins. Although low antimicrobial activity could be obtained from plant lectins, the information was still promising important for future research because nowadays extraction of bioactive compounds directly from their natural source is not the only way for the investigation. If the structure of the bioactive compound was elucidated, using knowledge on recombinant DNA technology could possibly produce a synthetic compound. And since antimicrobial-resistant organisms have been the major problem in medical treatment, searching for new antimicrobial compounds are still is interested.

#### **15. Acknowledgement**

The authors thank the Chulalongkorn University Graduate School thesis grant, the 90th Anniversary of Chulalongkorn University fund, the Thailand Research Fund, through the TRF-MAG window II, the National Research University Project of CHE, the Ratchadaphiseksomphot Endowment Fund (AM1019A, and AS613A), and the Thai Government Stimulus Package 2 (TKK2555), for financial support of this research, as well as the Institute of Biotechnology and Genetic Engineering for support and facilities.

#### **16. References**

166 Antimicrobial Agents

The unique property of lectins to bind noncovalently to simple sugars and therefore to polysaccharides and glycoconjugates has attracted the interest of virologists. In virology, lectins have been used for detection of viral glycoproteins in purified and infected cells, as well as for viral purification. Lectin studies have revealed information about the structure of viral glycoproteins, structures important in their pathogenicity. A significant contribution of lectin use in virology has been in the development of unique diagnostic methods that yield specific identification of viral agents. Purified influenza virus yields macroscopically visible flocculation when mixed with Concanavalin A. (Klenk et al., 1984) When influenza virus is treated with a proteolytic enzyme, the glycoprotein spikes of the virus are released. These treated viral particles no longer agglutinate with this lectin, but will flocculate in the presence of *N*-acetylgalactosamine-associated lectins, such as *Dolichos biflorus* or *Helix pomatia*. Other viruses, including arboviruses, vesicular stomatitis virus, paramyxoviruses, leukoviruses, and hepatitis B virus, also agglutinate with Concanavalin A. Concanavalin A was shown to block specifically adsorption of the bacteriophage binding sites of *Bacillus subtilis* possessing αglucosylated teichoic acids in the cell walls associated with teichoic acids. It was suggested that the application of this lectin might be useful as a means to correlated bacteriophage and

Biochemical and molecular studies of numerous lectins eventually demonstrated that only a limited number of carbohydrate-binding motifs evolved in plants (Peumans et al. 2000). Since the specificity of these binding motifs is primarily directed against foreign glycans, it is generally accepted now that many plant lectins are involved in the recognition and binding of glycans from foreign organisms, and accordingly play a role in plant defense (Peumans and Van Damme 1995; and Van Damme et al. 1998). Most plant lectins are probably involved in the plant's defense. Whereas direct interference with viruses and microorganisms are rather exceptional, the deleterious effects of plant lectins on predatory invertebrates and higher animals are obvious. Considering the abundance of lectins in storage organs and their storage protein-like behavior, we believe that plants accumulate part of their nitrogen reserve in the form of carbohydrate-binding proteins, which can be used as passive-defense proteins. Although low antimicrobial activity could be obtained from plant lectins, the information was still promising important for future research because nowadays extraction of bioactive compounds directly from their natural source is not the only way for the investigation. If the structure of the bioactive compound was elucidated, using knowledge on recombinant DNA technology could possibly produce a synthetic compound. And since antimicrobial-resistant organisms have been the major problem in

medical treatment, searching for new antimicrobial compounds are still is interested.

the Institute of Biotechnology and Genetic Engineering for support and facilities.

The authors thank the Chulalongkorn University Graduate School thesis grant, the 90th Anniversary of Chulalongkorn University fund, the Thailand Research Fund, through the TRF-MAG window II, the National Research University Project of CHE, the Ratchadaphiseksomphot Endowment Fund (AM1019A, and AS613A), and the Thai Government Stimulus Package 2 (TKK2555), for financial support of this research, as well as

serologic typing of staphylococci. (Archibald and Coapes, 1972).

**14. Conclusion** 

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**9** 

*France* 

**The Natural Antimicrobial** 

**Chromogranins/Secretogranins-Derived Peptides – Production, Lytic Activity and** 

Ménonvè Atindehou\*, Rizwan Aslam\*, Jean-François Chich,

Youssef Haïkel, Francis Schneider and Marie-Hélène Metz-Boutigue *Biomatériaux et Ingénierie Tissulaire, University of Strasbourg, Strasbourg* 

Multidrug-resistant organisms, such as methicillin-resistant *Staphylococcus aureus* (MRSA) and Vancomycin-resistant enterococci (VRE) have important infection control implications in all healthcare stings. Multidrug antibiotic resistance is a worldwide crucial health problem and the production of new potent antibiotics, acting alone or in combination is urgent. In addition, a major factor in the emergence of antibiotic resistant organisms is the overuse of antibiotics in the hospital or the community. To overcome this abuse, numerous efforts are undertaken to

Indeed, stimulating organism defense is a promising way to struggle against pathogens. The innate immune system is, since 2 billion years, the primary defense in most living organisms and antimicrobial peptides (AMPs) are fundamental components of the innate immune defense of multicellular organisms, either animal or vegetal (Bulet et al., 2004; Aerts et al.

The antimicrobial peptides (AMPs) have been well conserved throughout the evolution and they ensure the organism's defense against a large number of pathogens. They serve as endogenous antibiotics that are able to rapidly kill bacteria, fungi and viruses. Interestingly, they are not toxic for the host cells. Taking into consideration the diversity of the living beings, it is presumed that a large number of specific antibiotic peptides have been developed during evolution, allowing a protection of each organism in various conditions and the last years it has clearly appeared that many of these peptides, in addition to their direct antimicrobial activity, also have a wide range of functions in modulating both innate and adaptive immunity. Most of these are small molecules (less than 40 aminoacids) but some can be proteins. To date more than 1414 antibacterial, antifungal and 107 antiviral peptides have been

reduce antibiotics prescription and/or promote synergistic effects by others molecules.

**1. Introduction** 

2008; Manners, 2007).

 \*

**1.2 The antimicrobial peptides** 

These authors contributed equally

**1.1 Multidrug antibiotic resistance and innate immunity** 

**Processing by Bacterial Proteases** 

