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Publicly Available Published by De Gruyter June 1, 2013

Current and future use of “dried blood spot” analyses in clinical chemistry

Sylvain Lehmann, Constance Delaby, Jérôme Vialaret, Jacques Ducos and Christophe Hirtz


The analysis of blood spotted and dried on a matrix (i.e., “dried blood spot” or DBS) has been used since the 1960s in clinical chemistry; mostly for neonatal screening. Since then, many clinical analytes, including nucleic acids, small molecules and lipids, have been successfully measured using DBS. Although this pre-analytical approach represents an interesting alternative to classical venous blood sampling, its routine use is limited. Here, we review the application of DBS technology in clinical chemistry, and evaluate its future role supported by new analytical methods such as mass spectrometry.


Over a century since a new blood sampling method based on the use of a dry matrix was first described by Ivar Bang [1], the interest in dried blood spot technology has continuously evolved. This alternative approach, based on collecting blood spots on blotting paper and drying them, is called “dried blood spot” or DBS. In 1963, Robert Guthrie used this technique to develop systematic neonatal screening for the metabolic disease, phenylketonuria [2]. Set up for the first time in Scotland, this use of DBS spread to the UK in the 1970s, mainly to detect any innate errors in metabolism that were treatable. Of note, the use of DBS remains almost exclusively limited to this type of neonatal screening, even though many studies demonstrate its potential application in clinical biology, as well as in research. Indeed, classical clinical chemistry methods, small molecule and lipid analysis or molecular biology approaches, are all perfectly suited to the use of DBS. However, one limitation is represented by the small blood volumes associated with DBS sampling (5–10 µL) and therefore the need for very sensitive methods. Recent technological advances, in microfluidics, multiplex immunological/genomic detection systems, and mass spectrometry, could however settle most sensitivity problems. In this overview we will summarize the pros and cons of this particular biological sampling method and evaluate its future role in clinical biology.

General DBS procedure

Collection and sampling

The collection area (finger, heel) has to be first disinfected. The skin is then punctured with a sterile lancet (Figure 1). The first blood drop is dabbed and subsequent drops are placed on blotting paper marked with circles to be filled. Once all the required circles are filled, the blotting paper is left to dry for a few hours at room temperature on a non-absorbent surface. The drying time is very important as residual humidity favors bacterial development or molds and modifies the extraction stage [3].

Figure 1 
						DBS collection process.
						Peripheral blood is collected by the patient at home. He disinfects the area (finger) and pierces the skin using a sterile lancet before blotting the blood onto high quality filter paper. The DBS is dried for 1–3 h at room temperature and mailed using the classical envelope. At the laboratory, the DBS is stored at room temperature. The sample is punched (2–6 mm) and the analytes are extracted using an appropriate buffer before analysis.

Figure 1

DBS collection process.

Peripheral blood is collected by the patient at home. He disinfects the area (finger) and pierces the skin using a sterile lancet before blotting the blood onto high quality filter paper. The DBS is dried for 1–3 h at room temperature and mailed using the classical envelope. At the laboratory, the DBS is stored at room temperature. The sample is punched (2–6 mm) and the analytes are extracted using an appropriate buffer before analysis.


Once dry, the DBS cards are moved into a waterproof plastic bag, possibly along with a desiccant and a humidity indicator [4]. The purpose of the desiccant is to finalize the drying process, which also minimizes any risk of infection associated with sampling. Periods of storage at room temperature vary according to the biological factor, from 1 week for proteins [5], to 1 year or more for nucleic acids [6]. As far as serology is concerned, the blotting papers are usually kept at –20°C upon receipt [7]. For long-term preservation (up to several years) the blotting papers are stored either at −20°C or –80°C [8, 9].


Extraction of the analytes from DBS specimens needs to be achieved using a standard procedure. One or more 2–8 mm diameter discs are then created with a specific punch. These small “spots” are placed in an elution buffer for variable time spans according to the procedure. The DBS extraction is then treated as a hemolyzed whole blood sample, and tested with methods often intended for plasma or serum. The elution buffer plays a major role in re-solubilizing the analytes to be tested. A wide variety of buffers are described in the literature. The most common are saline/phosphate buffers, often with added detergents (Tween, Triton…), carrier proteins and chelators [ethylene diamine tetra acetic acid (EDTA)], as well as organic buffers with methanol, acetonitrile or ethanol. For nucleic acids, standard commercial kits exist which are compatible with molecular biology tests, from polymerase chain reaction (PCR) to genomic chips [10].

Pros and cons of DBS

One of the main advantages of using DBS technology is that it allows access to samples in pre-analytical situations were standard blood collection is challenging (problem with sampling, storage). The typical DBS contains approximately 50 µL of whole blood on an average surface of 12 mm2 (Figure 2). It enables the testing of various analytes such as nucleic acids, proteins, lipids, or small organic and non-organic molecules (Table 1). Two types of DBS are mostly available: cotton paper filters of different qualities (Whatmann 903 Protein Saver Cards Whatmann, Springfield Mill, UK; Perkin Elmer 226 Spot Saver Card, Perkin Elmer, Waltham, USA) and glass microfiber filter papers (Agilent Bond Elut DMS, Santa Clara, CA, USA; Sartorius Glass Microfiber Filters, Goettingen, Germany). The main difference between the two supports is that the glass fiber does not soak up reagents, which diminishes non-specific analyte adsorption on the membrane.

Figure 2 
					Comparison of the use of classical blood sampling versus DBS sampling resulting in a 100-fold reduction in blood volume and an ease of storage.

Figure 2

Comparison of the use of classical blood sampling versus DBS sampling resulting in a 100-fold reduction in blood volume and an ease of storage.

Table 1

Overview of DBS card usage in clinical chemistry other than its use for neonatal screening.

Methods Parameter Clinical interest References
Exogeneous nucleic acid
Real-time PCR

Human herpesvirus type 6 Differentiation active human herpesvirus type 6 infection from inherited HHV-6 [11, 12]
RT-PCR Human hepatitis C Monitoring hepatitis C virus (HCV) infection among injecting drug users [7, 13]
Real-time PCR Human hepatitis B Hepatitis B virus (HBV) DNA quantification [14]
Real-time PCR, Q-PCR Cytomegalovirus Diagnosis of human congenital cytomegalovirus infection [15, 16]
Nested PCR, RNA assays, RT-PCR HIV virus Detection of human immunodeficiency virus [8, 13, 17]
ELISA HIV virus Human immunodeficiency virus serotyping [18]
ELISA C-reactive protein Cardiovascular risk [19]
DELFIA Free-β human chorionic gonadotrophin (free-β hCG) and PAPP-A Fetal aneuploidy risk [20]
Immuno-fluorometric assays Luteinizing hormone and follicle-stimulating hormone Circulating gonadotropin concentrations [21]
Chemiluminescent immunoassay Prostate specific antigen (PSA) Prostate cancer screening [22]
RIA Somatedin-C (IGF-1) Screening test for growth hormone deficiency [23]
ELISA Apoliproteins B Hypercholesterolemia [24]
Immune nephelometry α1-Antitrypsin α1-Antitrypsin deficiency [5]
ELISA α-Fetoprotein Open neural tube defect and Down syndrome [25]
Enzyme assays Biotinidase Biotinidase deficiency [26]
EIA Calcitonin gene-related peptide Children with autism or mental retardation [27]
LC-MS/MS Ceruloplasmin Wilson’s disease [28]
Spectrophotometry Hemoglobin Folate analysis [29]
Turbidimetric immunoassay Glycated hemoglobin A1c Diagnosis and treatment of diabetes [30]
LC-MS/MS HbA2 Diagnosis of thalassemia [31]
Non-radiochemical HPLC Hypoxanthine-guanine phosphoribosyltransferase adenine phosphoribosyltransferase adenosine deaminase Purine metabolism disorders [32]
LC-MS/MS Iduronate 2-sulfatase Diagnosis of Hunter disease [33]
ELISA, RIA Insulin-like growth factor Evaluation of growth hormone status [34]
ELISA Prolactin Diagnosis of epilepsy [35]
ELISA Transferrin receptor Iron deficiency [36]
DELFIA Thyroglobulin Thyroid status [37]
ELISA CD4 CD4+ lymphocyte counts in HIV patients [38]
ELISA Measles and rubella IgM and IgG Detection of measles and rubella IgM and IgG [39]
DELFIA Toxoplasma gondii-specific IgM and IgA Screening of congenital toxoplasmosis [40]
RIA Insulin Diagnosis of hyperglycemia/hyper-insulinemia [41]
Enzyme assays Acid α-glucosidase Glycogen storage disease II [42]
Enzyme assays 8 lysosomal enzymes Clinical differentiation among mucopolysaccharidosis, oligosaccharidosis, and mucolipidosis II and III [43]
Enzyme assays α-iduronidase activity Diagnosis of α-L-iduronidase deficiency [44]
Biochemistry Phytanic acid and pristanic acid Diagnosis of peroxisomal disorders [45]
Electro-immunodiffusion β-Lipoprotein Familial type II and combined hyperlipidemia [46]
ELISA Fumarylacetoacetase Hereditary tyrosinemia type I [47]
Luminex TGF-β1, (MCP-1, (MIP-1α, MIP-1β, NT-4, BDNF, RANTES, CRP, MMP-9… Inflammatory status [48]
Enzyme immunoassay IgE Allergic disease and repeated macro-parasitic infections [49]
ELISA IgG and IgA Nasopharyngeal carcinoma screening [50]
Enzyme assays Lysosomal b-d-galactosidase (bG; EC Mucopolisaccharidosis type I [51]
Fluorometric immunoassay Thyroid-stimulating hormone Immunoreactive trypsin, creatine kinase MM isoenzyme Congenital hypothyroidism, congenital adrenal hyperplasia, and muscular dystrophy [52]
Column chromatography Thyroxine-binding globulin Neonatal hypothyroidism [53]
Immunoassay Trypsine immunoreactive (IRT) Cystic fibrosis [54]
ELISA Antibodies against hepatitis A Hepatitis A [55, 56]
ELISA Antibodies against hepatitis B Hepatitis B [57]
CORECELL Maternal antibody to hepatitis B Infection with HBV [58]
ELISA Anti-HCV antibodies Detection of antibodies to hepatitis C virus [59, 60]
ELISA Anti-malarial antibodies Diagnosis of malaria [61]
ELISA Pseudomonas aeruginosa antibodies Pseudomonas aeruginosa in patients with cystic fibrosis [62]
ELISA Thyroid antibody Thyroid-antibody screening [63]
ELISA Antibodies against tetanus Screening of tetanus and diphtheria toxins [64]
ELISA Antibodies against Brucella Diagnosis of human brucellosis [65]
ELISA Antibodies against cysticercus Detection of anti-cysticercus antibodies [66]
ELISA Antibody against HTLV-1 and HTLV-2 Detection of the Human T-lymphotropic virus [67]
Immuno-fluorescence Antibodies against to Coxiella burnetii, Bartonella quintana, and Rickettsia conorii Diagnosis of Rickettsial diseases [68]
ELISA Antibody against syphilis Diagnosis of syphilis [69]
Indirect hemagglutination test Antibody against Treponema Diagnosis of syphilis [70]
ELISA Antibody against Trypanosoma cruzi Diagnosis Trypanosoma cruzi infections [71]
ELISA Antibody against Trichomonas vaginalis Seroepidemiology of Trichomonas vaginalis [72]
Fluorescent Galactose-1-phosphate uridyltransferase (GALT) Galactosemia [73]
ELISA Epstein-Barr virus Epstein-Barr virus immunoglobulin G (IgG) serology [50]
EIA Rubella virus Detection of congenital Rubella virus [74]
EIA Dengue virus Dengue virus diagnosis [75]
ELISA Antibodies against hepatitis A Hepatitis A [55, 56]
ELISA Antibodies against hepatitis B Hepatitis B [57]
CORECELL Maternal antibody to hepatitis B Infection with HBV [58]
ELISA Anti-HCV antibodies Detection of antibodies to hepatitis C virus [59, 60]
Multiplex ligation-dependent probe amplification on DNA (MLPA) Detecting 22q11.2 deletions Manifestations associated with DiGeorge syndrome [76]
PCR GSTM1 et GSTT1 gene variant Researching pediatric cancer susceptibility genes [77]
ELISA multiplex Human papillomaviruses (HPV), Helicobacter pylori, hepatitis C virus (HCV), and JC polyomavirus (JCV) Infections of HPV, H. pylori, HCV, and JCV [78]
Lipids and small molecules
Densitometry Phenylalanine Phenylketonuria [2]
Enzymatic method Triglycerides Evaluation of the cardiometabolic risk [79]
LC-MS/MS Amino, organic, and fatty acid Metabolic disorders [80]
Fluorimetric HPLC method Homocysteine Homocysteinuria [81]
Enzymic methods Determination of glucose Monitoring of diabetic patients [82]
LC-MS/MS 17-OHP, androstenedione Congenital adrenal hyperplasia [83]
HPLC Retinol Retinol analysis [84]
LC-MS/MS Thyroxin (T4) and TSH Congenital hypothyroidism [85]
Chemiluminescence Free thyroxine (FT4) Assessment of thyroid status [86]
LC-MS/MS Free carnitine Inborn errors of metabolism [87]
GC-MS Methylcitrate Newborn screening for propionic acidemia [88]
GC-MS Octanoate, decanoate, cis-4-decenoic acid (C10:1) and cis-5-tetradecenoic acid Free fatty acids [89]
LC-MS/MS Succinylacetone Hepatorenal tyrosinemia [90]
FIA-ESI-MS/MS Guanidinoacetate and creatine Primary creatine disorders [91]
LC-MS HIV antiretroviral drugs

HIV therapeutic follow-up [92, 93]
RIA Cocaine metabolite (benzoylecgonine) Information on newborns and maternal exposures to various substances, including drugs of abuse [94]
LC/MS Quinine, mefloquine, sulfadoxine, pyrimethamine, lumefantrine, chloroquine Blood levels of drugs administered for malaria and pneumonia treatment [95, 96]
Capillary gas chromatography Dichlorodiphenyldichloroethylene Newborns’ body burden of environmental pollutants [97]
Fluorescence polarization immunoassay Theophylline Therapeutic drug monitoring [98]
PCR Mutations of factor V G1691A (FVL), prothrombin (PT) G20210A, 5′10′ methylenetetrahydrofolate reductase (MTHFR) C677T, and methionine synthase (MS) A2756G Susceptibility to venous thromboembolism [99]
Real-time PCR Mutation c.-32T>G (IVS1-13>G) Acid maltase deficiency [100]
DNA-based assay Mutation (IVS4+919G->A) Fabry disease [101]
DHPLC Substitution (c.840C>T) Spinal muscular dystrophy [102]
Specific restriction digest method Mutation (c.985A>G) Medium chain acyl-coA dehydrogenase deficiency (MCADD) [103]
PCR Mutation of cystic fibrosis transmembrane conductance regulator (CFTR) Cystic fibrosis [104]
PCR DNA mutation β-thalassemia [105]
PCR Real-time PCR SMN1 exon 7 deletions

Copy number variations of SMN1 and SMN2
Spinal muscular atrophy [106]
PCR FMR1 methylation Fragile X syndrome [107]
Multiplex ligation-dependent probe amplification on DNA (MLPA) Detecting 22q11.2 deletions Manifestations associated with DiGeorge syndrome [76]
PCR GSTM1 and GSTT1 gene variant Researching pediatric cancer susceptibility genes [77]

In comparison to conventional blood testing, DBS offers practical, clinical and financial advantages. Firstly, DBS collection is easy to perform and relatively painless (Figure 1). It can be carried out by the patient at home, without the need for specialized structures such as medical laboratories. This sampling procedure is far less invasive than venipuncture, therefore is better suited for patients requiring numerous blood tests, such as those with damaged/altered veins, the elderly or infants. The use of DBS also minimizes the volume of blood taken from patients. It has been shown that drying the blood spot on blotting paper damages the capsid of viruses [HIV, Cytomegalovirus (CMV), hepatitis C virus (HCV), human T-lymphotropic virus (HTLV)] [108] reducing any possible risk of contamination for medical or paramedical staff [4]. In addition, it enables the shipping of samples by regular mail with no particular risk of contamination. This represents a valuable asset for sampling in remote communities either located far away from a testing laboratory or with limited technical infrastructure available, therefore provides added value compared to standard blood sampling [59]. Through its small size and stacking capacity, DBS is also a valuable solution for reducing and facilitating storage in clinical laboratories and biobanks [109]. It is noteworthy that in case of storage, an individual bagging or a separation using a sturdy paper will be important to avoid the possibility of cross-contamination between cards [3]. These properties of DBS have been utilized in experimental research, by facilitating pharmacological studies and pharmacokinetics on small animals with very limited volumes of biological liquids. This follows the regulations aimed at protecting small animals (decreasing sample volume and sophistication of sampling methods) during pre-clinical studies [110]. Concerning sample stability, many studies have shown that most analytes from whole blood are stable at room temperature for at least 7 days. In some cases such as opiates, DBS even increases stability during storage [111], and nucleic acids are a major tool for short- and long-term preservation, as they can be isolated after several months at room temperature and several years at −20°C. [112]. From a medico-economical point of view, it is interesting to note that the use of DBS allows a significant cost reduction due to decreased requirements in trained staff, facilitated transportation, storage, and processing.

A major drawback of DBS technology resides in the nature of the biological sample itself (Figure 2). In a standard sampling procedure, either serum or plasma is analyzed, whereas DBS samples are composed of hemolyzed whole blood. Hence, interferences due to hemoglobin and the release of intracellular content could occur. The blood cells (erythrocytes, leukocytes, platelets etc.) are altered by the drying process, thus cellular hematological testing is impossible. Drying can also denature proteins and alters the enzymatic activity of blood proteins (aspartate transaminase). Any remaining cells in the samples can also change the global protein composition and therefore modify the concentration of some analytes. In some cases, clinical thresholds set up using standard blood samples need to be adapted. Hematocrit that affects blood dispersal on the blotting paper also needs to be taken into account [113]. The small volume of samples resulting from the DBS can be a disadvantage for low sensitivity assays [4] and for running multiple tests.

Use of DBS in clinical chemistry

The primary use of DBS in France is systematic neonatal screening. As blood sampling in newborns is difficult, DBS technology represents a viable alternative. DBS testing was set up in 1978 by the French Association for screening and preventing disabilities in children ( Sampling of newborns enables the detection of phenylketonuria, hypothyroidism, adrenal hyperplasia, cystic fibrosis and sickle cell disease (in some areas). The extension of these tests to cover a wider number of diseases, similar as in to USA, is currently under consideration [28]. A positive result will always be confirmed or denied by further specific tests. Beyond its use for neonatal screening, many clinical analytes can be measured using DBS. These analytes are divided into four major categories as follows (see also Table 1):

Exogenous nucleic acids

The measurement of nucleic acids is typically required in the virology field. There is a growing interest in viral screening through nucleic acid detection (RNA, DNA) using DBS, as current molecular biology technologies [quantitative polymerase chain reaction (Q-PCR), reverse transcription polymerase chain reaction (RT-PCR)] are very sensitive and require only a small sample amount (<20 µL). Nevertheless, it is important to note that the amount of material available from a DBS sample is between 1 and 2 logs lower compared to a standard serum or plasma sample. The preservation of nucleic acids on blotting paper is stable for long periods [3], providing it is dried and stored away from humidity in a suitable plastic bag containing a desiccant. DBS nucleic acid detection is mainly used in screening for viral diseases such as cytomegalovirus [15], herpes simplex virus [11], hepatitis A [55], hepatitis C [13] and HIV [114].

Peptides – proteins

Concerning proteins and peptides one caveat is represented by the relative difficulty of their extraction from DBS samples, as well as the low sensitivity of certain protein dosage. The main proteins measured from DBS can be classified into two groups: standard serum proteins and antibodies. The most widely used analytical techniques are immunological assays which measure clinical analytes with good specificities and sensitivities. An example is represented by the immunoturbidimetric assay for glycated hemoglobin (to monitor glycemic balance in diabetic patients). Glycated hemoglobin measured from DBS samples correlate well with standard tests. In addition, this analyte remains stable for over 15 days on DBS [30]. DBS is also well adapted for the enzyme-linked immunosorbent assay (ELISA) detection of specific antibodies against Epstein-Barr virus [50], Rubella virus [74], dengue virus [75] or hepatitis C [7, 59] and HIV virus [13].

An interesting evolution of liquid chromatography/mass spectrometry (LC/MS) is represented by quantitative techniques for measuring peptides and proteins [115]. This approach was adapted on DBS to measure ceruloplasmin for the neonatal screening of Wilson’s disease [28] and for peptide C quantification [116]. When used in multiplex mode (multiple reaction monitoring) this mass spectrometry method has the potential to measure many analytes within only a few microliters [115]. For instance, Chambers et al. [117] have succeeded in quantifying a panel of 40 serum proteins from DBS, using this approach.

Lipids, sugars and small molecules

Phenylalanine, an amino acid measured in phenylketonuria screening of newborns, exemplifies the dosage of small molecules using DBS [2]. Small organic molecules are significantly less sensitive than proteins to the drying process which characterizes DBS samples. In addition, the major progress of liquid chromatography/mass spectrometry (LC/MS) in this field has allowed the quantification of many small molecules such as vitamin D [118] or lipids [79]. For instance, high levels of triglycerides, representing an important risk for cardiovascular and coronary diseases, can be quantified using DBS. These analytes remain stable on DBS for 30 days at room temperature and up to 90 days at 4°C. The profiling of glycans on DBS was also recently achieved using mass spectrometry [119].


In 1993, Henderson et al. [120] demonstrated the use of DBS for detecting narcotics, such as cocaine, through modification of a radioimmunoassay (RIA) commercial kit. Xenobiotic testing using DBS has since played an important role, mainly by the screening of antimalarial and antiretroviral drugs by LC/MS in isolated populations [95]. Another example is represented by the quantification of nine antiretroviral molecules in HIV using DBS. This detection method has been validated by the Food and Drug Administration (FDA) with sample stability ranging from 12 to over 90 days at room temperature [92]. In the field of toxicology, which is a major application of DBS [121], Saussereau et al. [122] have, for example, developed a new drug screening method based on LC/MS using on-line extraction for the quantification of opiates, cocainics or amphetamines. The development of these new measurement techniques, based on LC/MS for xenobiotics, will greatly increase the interest of using DBS in clinical chemistry.


The clinical potential of DBS for genomics has been demonstrated as early as 1987 [123]. DNA micro-extraction from dried blood has allowed the detection of mutations responsible for diseases such as cystic fibrosis [124], X fragile syndrome [107], spinal muscular atrophy [106], cancers [77] and thalassemia [105]. DBS, which is a fairly inexpensive sampling and storage method, is also a good choice for genetic material biobanks [125]. For instance, the Danish national biobank for neonatal screening includes over 2 million DBS which virtually corresponds to all Danish people born since 1982.


The use of DBS has many advantages in terms of sampling, transportation, storage and biosafety when compared to classical collection methods. One interesting aspect of DBS is the possibility of simplified “self/home blood sampling”. The patient will be able to independently and safely collect a blood sample. The DBS will then be sent to the laboratory by mail. As described in this review, many clinical analytes are already available on DBS, and more are to follow, thanks to innovative approaches. Indeed, development of microfluidics, multiplex immunological/genomic detection systems, mass spectrometry and automated DBS processing open new interesting clinical prospects. The detection and follow-up of metabolic, infectious and chronic diseases could therefore rely on the use of DBS. Both the patient and society could benefit from this technology. Already, several public and commercial laboratories in both Europe and USA are offering DBS kits for a broad range of analytes often grouped into panels for hormonal, metabolic or cardiovascular diseases. This evolution could dramatically change how clinical chemistry pre-analytics are handled in the future.

Corresponding author: Sylvain Lehmann, CHU Montpellier, IRB, 80 Avenue Augustin Fliche, Montpellier 34295, France, E-mail:

The authors thank Rachel Almeras, Bader Al Taweel, Domitille Héron and Thibault Fortane for their initial help in the writing of this review and Brigitte Lehmann for editing the manuscript.

Conflict of interest statement

Authors’ conflict of interest disclosure: The authors stated that there are no conflicts of interest regarding the publication of this article.

Research funding: None declared.

Employment or leadership: None declared.

Honorarium: None declared.


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Received: 2013-03-26
Accepted: 2013-04-19
Published Online: 2013-06-01
Published in Print: 2013-10-01

©2013 by Walter de Gruyter Berlin Boston

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